BLASTP 2.2.1 [Apr-13-2001]
Reference:
Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schäffer,
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997),
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs", Nucleic Acids Res. 25:3389-3402.
Query= gi|15645139|ref|NP_207309.1| glutamine synthetase (glnA)
[Helicobacter pylori 26695]
(481 letters)
Database: /var/www/html/HP/blast_new/blast/db/pdbaa
13,198 sequences; 2,899,336 total letters
Searching...........................done
Score E
Sequences producing significant alignments: (bits) Value
pdb|1F52|A Chain A, Crystal Structure Of Glutamine Syntheta... 442 e-125
pdb|2GLS|A Chain A, Refined Atomic Model Of Glutamine Synth... 442 e-125
pdb|1HTO|A Chain A, Crystallographic Structure Of A Relaxed... 400 e-112
pdb|1FMI|A Chain A, Crystal Structure Of Human Class I Alph... 33 0.092
pdb|1FO2|A Chain A, Crystal Structure Of Human Class I Alph... 33 0.092
pdb|1FHE| Glutathione Transferase (Fh47) From Fasciola He... 32 0.21
pdb|1CB8|A Chain A, Chondroitinase Ac Lyase From Flavobacte... 31 0.35
pdb|1HM2|A Chain A, Active Site Of Chondroitinase Ac Lyase ... 31 0.35
pdb|1JCI|A Chain A, Stabilization Of The Engineered Cation-... 28 2.3
pdb|4CCX| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt... 28 2.3
pdb|3CCX| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt... 28 2.3
pdb|1KXM|A Chain A, Crystal Structure Of Cytochrome C Perox... 28 2.3
pdb|1CYF| Mol_id: 1; Molecule: Cytochrome C Peroxidase; C... 28 2.3
pdb|1CCJ| Conformer Selection By Ligand Binding Observed ... 28 2.3
pdb|2CEP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant W... 28 2.3
pdb|1CCK| Altering Substrate Specificity Of Cytochrome C ... 28 2.3
pdb|7CCP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant W... 28 2.3
pdb|1CMU| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5... 28 2.3
pdb|1CCG| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt... 28 2.3
pdb|1CCA| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5... 28 2.3
pdb|2CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mu... 28 2.3
pdb|1AA4| Specificity Of Ligand Binding In A Buried Polar... 28 2.3
pdb|1CCL| Probing The Strength And Character Of An Asp-Hi... 28 2.3
pdb|6CCP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant W... 28 2.3
pdb|1KRJ|A Chain A, Engineering Calcium-Binding Site Into C... 28 2.3
pdb|1DSE|A Chain A, Cytochrome C Peroxidase H175g Mutant, I... 28 2.3
pdb|1DS4|A Chain A, Cytochrome C Peroxidase H175g Mutant, I... 28 2.3
pdb|1A2G| Probing The Strength And Character Of An Asp-Hi... 28 2.3
pdb|4CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mu... 28 2.3
pdb|1KOK|A Chain A, Crystal Structure Of Mesopone Cytochrom... 28 2.3
pdb|1BVA|A Chain A, Manganese Binding Mutant In Cytochrome ... 28 2.3
pdb|1CPE| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant W... 28 2.3
pdb|1DJ5|A Chain A, Crystal Structure Of R48a Mutant Of Cyt... 28 2.3
pdb|1A2F| Probing The Strength And Character Of An Asp-Hi... 28 2.3
pdb|3CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mu... 28 2.3
pdb|1CPG| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant W... 28 2.3
pdb|2PCC|A Chain A, Yeast Cytochrome C Peroxidase (Ccp) Com... 28 2.3
pdb|1CCC| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5... 28 2.3
pdb|1JDR|A Chain A, Crystal Structure Of A Proximal Domain ... 28 2.3
pdb|5CCP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant W... 28 2.3
pdb|1KXN|A Chain A, Crystal Structure Of Cytochrome C Perox... 28 2.3
pdb|1CCB| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5... 28 2.3
pdb|1FY3|A Chain A, [g175q]hbp, A Mutant Of Human Heparin B... 27 3.9
pdb|1AE5| Human Heparin Binding Protein 27 3.9
pdb|4GTU|A Chain A, Ligand-Free Homodimeric Human Glutathio... 27 5.1
pdb|1AC4| Variation In The Strength Of A Ch To O Hydrogen... 26 8.6
pdb|1BEM| Interaction Between Proximal And Distals Region... 26 8.6
pdb|1EBE|A Chain A, Laue Diffraction Study On The Structure... 26 8.6
pdb|1BEJ| Interaction Between Proximal And Distals Region... 26 8.6
pdb|1BEK| Effect Of Unnatural Heme Substitution On Kineti... 26 8.6
pdb|1BES| Interaction Between Proximal And Distals Region... 26 8.6
pdb|1BEP| Effect Of Unnatural Heme Substitution On Kineti... 26 8.6
>pdb|1F52|A Chain A, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|B Chain B, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|C Chain C, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|D Chain D, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|E Chain E, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|F Chain F, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|G Chain G, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|H Chain H, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|I Chain I, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|J Chain J, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|K Chain K, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F52|L Chain L, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium Co-Crystallized With Adp
pdb|1F1H|A Chain A, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|B Chain B, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|C Chain C, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|D Chain D, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|E Chain E, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|F Chain F, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|G Chain G, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|H Chain H, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|I Chain I, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|J Chain J, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|K Chain K, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1F1H|L Chain L, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Thallium Ions
pdb|1FPY|A Chain A, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|B Chain B, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|C Chain C, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|D Chain D, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|E Chain E, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|F Chain F, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|G Chain G, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|H Chain H, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|I Chain I, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|J Chain J, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|K Chain K, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|1FPY|L Chain L, Crystal Structure Of Glutamine Synthetase From Salmonella
Typhimurium With Inhibitor Phosphinothricin
pdb|2LGS|A Chain A, Glutamine Synthetase (E.C.6.3.1.2) Complexed With
Glutamate
pdb|1LGR| Glutamine Synthetase (E.C.6.3.1.2) Complexed With Amp
Length = 468
Score = 442 bits (1137), Expect = e-125
Identities = 227/461 (49%), Positives = 301/461 (65%), Gaps = 5/461 (1%)
Query: 21 ENEVEFVDFRFSDIKGTWNHIAYSFGALTHGMLKEGIPFDASCFKGWQGIEHSDMILTPD 80
E+EV+FVD RF+D KG H+ + +EG FD S GW+GI SDM+L PD
Sbjct: 11 EHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKGINESDMVLMPD 70
Query: 81 LVRYFIDPFSADVSVVVFCDVYDVYKNQPYEKCPRSIAKKALQHLKDSGLGDVAYFGAEN 140
IDPF AD ++++ CD+ + Q Y++ PRSIAK+A +L+ +G+ D FG E
Sbjct: 71 ASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRATGIADTVLFGPEP 130
Query: 141 EFFIFDSIKIKDASNSQYYEVDSEEGEWNRDRSFENGVNFGHRPGKQGGYMPVPPTDTMM 200
EFF+FD I+ + + + +D EG WN +E G N GHRPG +GGY PVPP D+
Sbjct: 131 EFFLFDDIRFGASISGSHVAIDDIEGAWNSSTKYEGG-NKGHRPGVKGGYFPVPPVDSAQ 189
Query: 201 DIRTEIVKVLNQVGLETFVVHHEVAQA-QGEVGVKFGDLVEAADNVQKLKYVVKMVAHLN 259
DIR+E+ V+ Q+GL HHEVA A Q EV +F + + AD +Q KYVV VAH
Sbjct: 190 DIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRF 249
Query: 260 GKTATFMPKPLYGDNGSGMHTHVSVWKNNENLFSGETYKGLSEFALHFLGGVLRHARGLA 319
GKTATFMPKP++GDNGSGMH H+S+ KN NLFSG+ Y GLSE AL+++GGV++HA+ +
Sbjct: 250 GKTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAKAIN 309
Query: 320 AFTNASTNSYKRLIPGYEAPSILTYSANNRSASVRIPYGISKNSARFEFRFPDSSSNPYL 379
A N +TNSYKRL+PGYEAP +L YSA NRSAS+RIP S + R E RFPD ++NPYL
Sbjct: 310 ALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVASPKARRIEVRFPDPAANPYL 369
Query: 380 AFAAILMAGMDGVKNKIDPGEAMDINLFKLTLDEIREKGIKQMPHTLRRSLEEMLADKQY 439
FAA+LMAG+DG+KNKI PGE MD NL+ L +E +E I Q+ +L +L + D+++
Sbjct: 370 CFAALLMAGLDGIKNKIHPGEPMDKNLYDLPPEEAKE--IPQVAGSLEEALNALDLDREF 427
Query: 440 LKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFITTYS 480
LK VF++E I AY +L+ E PHP EF YS
Sbjct: 428 LKAGGVFTDEAIDAYIALR-REEDDRVRMTPHPVEFELYYS 467
>pdb|2GLS|A Chain A, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|B Chain B, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|C Chain C, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|D Chain D, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|E Chain E, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|F Chain F, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|G Chain G, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|H Chain H, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|I Chain I, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|J Chain J, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|K Chain K, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
pdb|2GLS|L Chain L, Refined Atomic Model Of Glutamine Synthetase At 3.5
Angstroms Resolution
Length = 469
Score = 442 bits (1137), Expect = e-125
Identities = 227/461 (49%), Positives = 301/461 (65%), Gaps = 5/461 (1%)
Query: 21 ENEVEFVDFRFSDIKGTWNHIAYSFGALTHGMLKEGIPFDASCFKGWQGIEHSDMILTPD 80
E+EV+FVD RF+D KG H+ + +EG FD S GW+GI SDM+L PD
Sbjct: 12 EHEVKFVDLRFTDTKGKEQHVTIPAHQVNAEFFEEGKMFDGSSIGGWKGINESDMVLMPD 71
Query: 81 LVRYFIDPFSADVSVVVFCDVYDVYKNQPYEKCPRSIAKKALQHLKDSGLGDVAYFGAEN 140
IDPF AD ++++ CD+ + Q Y++ PRSIAK+A +L+ +G+ D FG E
Sbjct: 72 ASTAVIDPFFADSTLIIRCDILEPGTLQGYDRDPRSIAKRAEDYLRATGIADTVLFGPEP 131
Query: 141 EFFIFDSIKIKDASNSQYYEVDSEEGEWNRDRSFENGVNFGHRPGKQGGYMPVPPTDTMM 200
EFF+FD I+ + + + +D EG WN +E G N GHRPG +GGY PVPP D+
Sbjct: 132 EFFLFDDIRFGASISGSHVAIDDIEGAWNSSTKYEGG-NKGHRPGVKGGYFPVPPVDSAQ 190
Query: 201 DIRTEIVKVLNQVGLETFVVHHEVAQA-QGEVGVKFGDLVEAADNVQKLKYVVKMVAHLN 259
DIR+E+ V+ Q+GL HHEVA A Q EV +F + + AD +Q KYVV VAH
Sbjct: 191 DIRSEMCLVMEQMGLVVEAHHHEVATAGQNEVATRFNTMTKKADEIQIYKYVVHNVAHRF 250
Query: 260 GKTATFMPKPLYGDNGSGMHTHVSVWKNNENLFSGETYKGLSEFALHFLGGVLRHARGLA 319
GKTATFMPKP++GDNGSGMH H+S+ KN NLFSG+ Y GLSE AL+++GGV++HA+ +
Sbjct: 251 GKTATFMPKPMFGDNGSGMHCHMSLAKNGTNLFSGDKYAGLSEQALYYIGGVIKHAKAIN 310
Query: 320 AFTNASTNSYKRLIPGYEAPSILTYSANNRSASVRIPYGISKNSARFEFRFPDSSSNPYL 379
A N +TNSYKRL+PGYEAP +L YSA NRSAS+RIP S + R E RFPD ++NPYL
Sbjct: 311 ALANPTTNSYKRLVPGYEAPVMLAYSARNRSASIRIPVVASPKARRIEVRFPDPAANPYL 370
Query: 380 AFAAILMAGMDGVKNKIDPGEAMDINLFKLTLDEIREKGIKQMPHTLRRSLEEMLADKQY 439
FAA+LMAG+DG+KNKI PGE MD NL+ L +E +E I Q+ +L +L + D+++
Sbjct: 371 CFAALLMAGLDGIKNKIHPGEPMDKNLYDLPPEEAKE--IPQVAGSLEEALNALDLDREF 428
Query: 440 LKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFITTYS 480
LK VF++E I AY +L+ E PHP EF YS
Sbjct: 429 LKAGGVFTDEAIDAYIALR-REEDDRVRMTPHPVEFELYYS 468
>pdb|1HTO|A Chain A, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|B Chain B, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|C Chain C, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|D Chain D, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|E Chain E, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|F Chain F, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|G Chain G, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|H Chain H, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|I Chain I, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|J Chain J, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|K Chain K, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|L Chain L, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|M Chain M, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|N Chain N, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|O Chain O, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|P Chain P, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|Q Chain Q, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|R Chain R, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|S Chain S, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|T Chain T, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|U Chain U, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|V Chain V, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|W Chain W, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTO|X Chain X, Crystallographic Structure Of A Relaxed Glutamine
Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|A Chain A, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|B Chain B, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|C Chain C, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|D Chain D, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|E Chain E, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|F Chain F, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|G Chain G, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|H Chain H, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|I Chain I, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|J Chain J, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|K Chain K, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|L Chain L, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|M Chain M, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|N Chain N, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|O Chain O, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|P Chain P, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|Q Chain Q, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|R Chain R, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|S Chain S, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|T Chain T, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|U Chain U, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|V Chain V, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|W Chain W, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
pdb|1HTQ|X Chain X, Multicopy Crystallographic Structure Of A Relaxed
Glutamine Synthetase From Mycobacterium Tuberculosis
Length = 477
Score = 400 bits (1028), Expect = e-112
Identities = 212/477 (44%), Positives = 290/477 (60%), Gaps = 7/477 (1%)
Query: 8 SESKIKEFFEFCKENEVEFVDFRFSDIKGTWNHIAYSFGALTHGMLKEGIPFDASCFKGW 67
+E + F+ K+ +VE+VD RF D+ G H A + +G+ FD S +G+
Sbjct: 1 TEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAFDGSSIRGF 60
Query: 68 QGIEHSDMILTPDLVRYFIDPFSADVSVVVFCDVYDVYKNQPYEKCPRSIAKKALQHLKD 127
Q I SDM+L PD IDPF A ++ + V+D + +PY + PR+IA+KA +L
Sbjct: 61 QSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIARKAENYLIS 120
Query: 128 SGLGDVAYFGAENEFFIFDSIKIKDASNSQYYEVDSEEGEWNRDRSFE--NGVNFGHRPG 185
+G+ D AYFGAE EF+IFDS+ +N +YEVD+ G WN + E N G++
Sbjct: 121 TGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWWNTGAATEADGSPNRGYKVR 180
Query: 186 KQGGYMPVPPTDTMMDIRTEIVKVLNQVGLETFVVHHEVAQ-AQGEVGVKFGDLVEAADN 244
+GGY PV P D +D+R +++ L G HHEV Q E+ +F L+ AAD+
Sbjct: 181 HKGGYFPVAPNDQYVDLRDKMLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADD 240
Query: 245 VQKLKYVVKMVAHLNGKTATFMPKPLYGDNGSGMHTHVSVWKNNENLFSGET-YKGLSEF 303
+Q KY++K A NGKT TFMPKPL+GDNGSGMH H S+WK+ L ET Y GLS+
Sbjct: 241 MQLYKYIIKNTAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDT 300
Query: 304 ALHFLGGVLRHARGLAAFTNASTNSYKRLIPGYEAPSILTYSANNRSASVRIPY-GISKN 362
A H++GG+L HA L AFTN + NSYKRL+PGYEAP L YS NRSA VRIP G +
Sbjct: 301 ARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNPK 360
Query: 363 SARFEFRFPDSSSNPYLAFAAILMAGMDGVKNKIDPGEAMDINLFKLTLDEIREKGIKQM 422
+ R EFR PDSS NPYLAF+A+LMAG+DG+KNKI+P +D +L++L +E I Q
Sbjct: 361 AKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEE--AASIPQT 418
Query: 423 PHTLRRSLEEMLADKQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFITTY 479
P L ++ + AD +YL E VF+ + I+ + S K E+ P +PHP+EF Y
Sbjct: 419 PTQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEPVNIRPHPYEFALYY 475
>pdb|1FMI|A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase
Length = 458
Score = 32.7 bits (73), Expect = 0.092
Identities = 21/74 (28%), Positives = 32/74 (42%), Gaps = 2/74 (2%)
Query: 285 WKNNENLFSGETYKGLSEFALHFLGGVLR--HARGLAAFTNASTNSYKRLIPGYEAPSIL 342
W + + F + L E + LGG+L H G + F + + RL+P + PS +
Sbjct: 74 WVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGNRLMPAFRTPSKI 133
Query: 343 TYSANNRSASVRIP 356
YS N V P
Sbjct: 134 PYSDVNIGTGVAHP 147
>pdb|1FO2|A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In
Complex With 1-Deoxymannojirimycin
pdb|1FO3|A Chain A, Crystal Structure Of Human Class I Alpha1,2-Mannosidase In
Complex With Kifunensine
Length = 460
Score = 32.7 bits (73), Expect = 0.092
Identities = 21/74 (28%), Positives = 32/74 (42%), Gaps = 2/74 (2%)
Query: 285 WKNNENLFSGETYKGLSEFALHFLGGVLR--HARGLAAFTNASTNSYKRLIPGYEAPSIL 342
W + + F + L E + LGG+L H G + F + + RL+P + PS +
Sbjct: 74 WVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGNRLMPAFRTPSKI 133
Query: 343 TYSANNRSASVRIP 356
YS N V P
Sbjct: 134 PYSDVNIGTGVAHP 147
>pdb|1FHE| Glutathione Transferase (Fh47) From Fasciola Hepatica
Length = 217
Score = 31.6 bits (70), Expect = 0.21
Identities = 19/65 (29%), Positives = 36/65 (55%), Gaps = 8/65 (12%)
Query: 399 GEAMDINL------FKLTLDEIREKGIKQMPHTLRRSLEEMLADKQYLKESQVFSEEFIQ 452
G AMD+ + + +E++E+ +K++P TL + + L D+ YL S V +F+
Sbjct: 96 GAAMDLRIGFGRVCYNPKFEEVKEEYVKELPKTL-KMWSDFLGDRHYLTGSSVSHVDFM- 153
Query: 453 AYQSL 457
Y++L
Sbjct: 154 LYETL 158
>pdb|1CB8|A Chain A, Chondroitinase Ac Lyase From Flavobacterium Heparinum
Length = 678
Score = 30.8 bits (68), Expect = 0.35
Identities = 37/160 (23%), Positives = 63/160 (39%), Gaps = 18/160 (11%)
Query: 128 SGLGDVAYFGAENEFFIF-DSIKIKDASNSQY-YEVDSEEGEW---NRDRS--------F 174
+G G + F A+ +F++ D+I + S++G W N S F
Sbjct: 482 TGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQSQKGNWFHINNSHSKDEVSGDVF 541
Query: 175 ENGVNFGHRP-GKQGGYMPVPPTDTMMDIRT---EIVKVLNQVGLETFVVHHEVAQAQGE 230
+ +N G RP Q Y+ +P + +I+ KVL V H ++ Q
Sbjct: 542 KLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAPKVLANTNQLQAVYHQQLDMVQA- 600
Query: 231 VGVKFGDLVEAADNVQKLKYVVKMVAHLNGKTATFMPKPL 270
+ G L A ++ K ++ H+NGK + PL
Sbjct: 601 IFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAADPL 640
>pdb|1HM2|A Chain A, Active Site Of Chondroitinase Ac Lyase Revealed By The
Structure Of Enzyme-Oligosaccharide Complexes And
Mutagenesis
pdb|1HMU|A Chain A, Active Site Of Chondroitinase Ac Lyase Revealed By The
Structure Of Enzyme-Oligosaccharide Complexes And
Mutagenesis
pdb|1HM3|A Chain A, Active Site Of Chondroitinase Ac Lyase Revealed By The
Structure Of Enzyme-Oligosaccharide Complexes And
Mutagenesis
pdb|1HMW|A Chain A, Active Site Of Chondroitinase Ac Lyase Revealed By The
Structure Of Enzyme-Oligosaccharide Complexes And
Mutagenesis
Length = 700
Score = 30.8 bits (68), Expect = 0.35
Identities = 37/160 (23%), Positives = 63/160 (39%), Gaps = 18/160 (11%)
Query: 128 SGLGDVAYFGAENEFFIF-DSIKIKDASNSQY-YEVDSEEGEW---NRDRS--------F 174
+G G + F A+ +F++ D+I + S++G W N S F
Sbjct: 504 TGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQSQKGNWFHINNSHSKDEVSGDVF 563
Query: 175 ENGVNFGHRP-GKQGGYMPVPPTDTMMDIRT---EIVKVLNQVGLETFVVHHEVAQAQGE 230
+ +N G RP Q Y+ +P + +I+ KVL V H ++ Q
Sbjct: 564 KLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAPKVLANTNQLQAVYHQQLDMVQA- 622
Query: 231 VGVKFGDLVEAADNVQKLKYVVKMVAHLNGKTATFMPKPL 270
+ G L A ++ K ++ H+NGK + PL
Sbjct: 623 IFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAADPL 662
>pdb|1JCI|A Chain A, Stabilization Of The Engineered Cation-Binding Loop In
Cytochrome C Peroxidase (Ccp)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|4CCX| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With
Met-Lys-Thr Inserted At The N-Terminus, Thr 53 Replaced
By Ile, Ala 147 Replaced By Met, Asp 152 Replaced By Gly
(Ins(M1,K2,T3),T53i,A147m,D152g)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|3CCX| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With
Met-Lys-Thr Inserted At The N-Terminus, Thr 52 Replaced
By Ile, Ala 147 Replaced By Tyr, Asp 152 Replaced By Gly
(Ins(M1,K2,T3),T52i,A147y,D152g)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|1KXM|A Chain A, Crystal Structure Of Cytochrome C Peroxidase With A
Proposed Electron Transfer Pathway Excised To Form A
Ligand Binding Channel
Length = 290
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 245 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 284
>pdb|1CYF| Mol_id: 1; Molecule: Cytochrome C Peroxidase; Chain: Null; Ec:
1.11.1.5; Engineered: Yes; Mutation: Ins(Met Ile At
N-Terminus), C128a, A193c
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1CCJ| Conformer Selection By Ligand Binding Observed With Protein
Crystallography
pdb|1CCI| How Flexible Are Proteins? Trapping Of A Flexible Loop
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|2CEP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Met 230 Replaced By Ile (Mi,M230i)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1CCK| Altering Substrate Specificity Of Cytochrome C Peroxidase Towards
A Small Molecular Substrate Peroxidase By Substituting
Tyrosine For Phe 202
Length = 291
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 285
>pdb|7CCP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Arg 48 Replaced By Leu (Mi,R48l)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1CMU| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With
Initial Met, Lys, Thr And With Trp 191 Replaced By Gly
And Asp 235 Replaced By Asn (Ins(M1,K2,T3),W191g,D235n)
And Soaked In 40 Millimolar Potassium (K+)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|1CCG| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With His
175 Replaced By Gly (H175g) Complexed With Imidazole
pdb|1CCE| Cytochrome C Peroxidase (E.C.1.11.1.5) (Ccp-Mkt) Mutant With His
175 Replaced By Gly (H175g)
Length = 291
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 285
>pdb|1CCA| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Wild Type
Length = 297
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 252 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 291
>pdb|2CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mutant With Asp 235
Replaced By Asn (D235N)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1AA4| Specificity Of Ligand Binding In A Buried Polar Cavity Of
Cytochrome C Peroxidase
pdb|1RYC| Cytochrome C Peroxidase W191g From Saccharomyces Cerevisiae
pdb|1CMP| Cytochrome C Peroxidase (Recombinant Yeast, Ccp-Mkt)
(E.C.1.11.1.5) Mutant With Trp 191 Replaced By Gly
(W191g) Complexed With 1,2-Dimethylimadazole
pdb|1CMT| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With
Initial Met, Lys, Thr And With Trp 191 Replaced By Gly
(Ins(M1,K2,T3),W191g) And Soaked In 40 Millimolar
Potassium (K+)
pdb|1CMQ| Cytochrome C Peroxidase (Recombinant Yeast, Ccp-Mkt)
(E.C.1.11.1.5) Mutant With Trp 191 Replaced By Gly
(W191g)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|1CCL| Probing The Strength And Character Of An Asp-His-X Hydrogen Bond
By Introducing Buried Charges
Length = 291
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 285
>pdb|6CCP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Arg 48 Replaced By Lys (Mi,R48k)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1KRJ|A Chain A, Engineering Calcium-Binding Site Into Cytochrome C
Peroxidase (Ccp)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|1DSE|A Chain A, Cytochrome C Peroxidase H175g Mutant, Imidazole Complex,
With Phosphate Bound, Ph 6, 100k
Length = 292
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 247 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 286
>pdb|1DS4|A Chain A, Cytochrome C Peroxidase H175g Mutant, Imidazole Complex,
Ph 6, 100k
pdb|1DSO|A Chain A, Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At
Ph 6, Room Temperature.
pdb|1DSP|A Chain A, Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At
Ph 7, Room Temperature.
pdb|1DSG|A Chain A, Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At
Ph 5, Room Temperature
Length = 292
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 247 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 286
>pdb|1A2G| Probing The Strength And Character Of An Asp-His-X Hydrogen Bond
By Introducing Buried Charges
Length = 291
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 285
>pdb|4CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mutant With Trp 51
Replaced By Phe (W51F)
Length = 293
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 248 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 287
>pdb|1KOK|A Chain A, Crystal Structure Of Mesopone Cytochrome C Peroxidase
(Mpccp)
pdb|2CYP| Cytochrome c Peroxidase (E.C.1.11.1.5) (Ferrocytochrome c (Colon)
H2O2 Reductase)
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|1BVA|A Chain A, Manganese Binding Mutant In Cytochrome C Peroxidase
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|1CPE| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Trp 191 Replaced By Gly (Mi,W191g)
Complexed With A Potassium Ion (K+)
pdb|1CPD| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Trp 191 Replaced By Gly (Mi,W191g)
Complexed With An Ammonium Ion (Nh4+)
pdb|1CPF| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Trp 191 Replaced By Gly (Mi,W191g)
Complexed With A Tris (+) Ion
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1DJ5|A Chain A, Crystal Structure Of R48a Mutant Of Cytochrome C
Peroxidase With N-Hydroxyguanidine Bound
pdb|1DJ1|A Chain A, Crystal Structure Of R48a Mutant Of Cytochrome C
Peroxidase
Length = 291
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 285
>pdb|1A2F| Probing The Strength And Character Of An Asp-His-X Hydrogen Bond
By Introducing Buried Charges
Length = 291
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 285
>pdb|3CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5) Mutant With Trp 191
Replaced By Phe (W191F)
pdb|1DCC| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Trp 191 Replaced By Phe (Mi,W191f)
Complexed With Dioxygen
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1CPG| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And Trp 191 Replaced By Gln (Mi,W191q)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|2PCC|A Chain A, Yeast Cytochrome C Peroxidase (Ccp) Complex With Yeast
Iso-1-Cytochrome C
pdb|2PCC|C Chain C, Yeast Cytochrome C Peroxidase (Ccp) Complex With Yeast
Iso-1-Cytochrome C
pdb|2PCB|A Chain A, Yeast Cytochrome C Peroxidase (Ccp) Complex With Horse
Heart Cytochrome C
pdb|2PCB|C Chain C, Yeast Cytochrome C Peroxidase (Ccp) Complex With Horse
Heart Cytochrome C
pdb|1CCP| Yeast Cytochrome c Peroxidase (E.C.1.11.1.5)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1CCC| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With Asp
235 Replaced By Ala (D235a)
Length = 297
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 252 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 291
>pdb|1JDR|A Chain A, Crystal Structure Of A Proximal Domain Potassium Binding
Variant Of Cytochrome C Peroxidase
Length = 294
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 288
>pdb|5CCP| Cytochrome C Peroxidase (E.C.1.11.1.5) Mutant With Met Ile Added
At N-Terminus And His 52 Replaced By Leu (Mi,H52l)
Length = 296
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 251 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 290
>pdb|1KXN|A Chain A, Crystal Structure Of Cytochrome C Peroxidase With A
Proposed Electron Transfer Pathway Excised To Form A
Ligand Binding Channel
Length = 289
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 244 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 283
>pdb|1CCB| Cytochrome C Peroxidase (Ccp-Mkt) (E.C.1.11.1.5) Mutant With Asp
235 Replaced By Glu (D235e)
Length = 297
Score = 28.1 bits (61), Expect = 2.3
Identities = 14/41 (34%), Positives = 22/41 (53%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L N FP + P PF F T
Sbjct: 252 KEYANDQDKFFKDFSKAFEKLLENGITFP-KDAPSPFIFKT 291
>pdb|1FY3|A Chain A, [g175q]hbp, A Mutant Of Human Heparin Binding Protein
(Cap37)
Length = 225
Score = 27.3 bits (59), Expect = 3.9
Identities = 17/58 (29%), Positives = 23/58 (39%), Gaps = 4/58 (6%)
Query: 306 HFLGGVLRHARGLAAFTNASTNSYKRLIPGYEAPSILTYSANNRSASVRIPYGISKNS 363
HF GG L HAR F + + ++ PG + Y R R + IS S
Sbjct: 24 HFCGGALIHAR----FVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISSMS 77
>pdb|1AE5| Human Heparin Binding Protein
Length = 225
Score = 27.3 bits (59), Expect = 3.9
Identities = 17/58 (29%), Positives = 23/58 (39%), Gaps = 4/58 (6%)
Query: 306 HFLGGVLRHARGLAAFTNASTNSYKRLIPGYEAPSILTYSANNRSASVRIPYGISKNS 363
HF GG L HAR F + + ++ PG + Y R R + IS S
Sbjct: 24 HFCGGALIHAR----FVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISSMS 77
>pdb|4GTU|A Chain A, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|B Chain B, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|C Chain C, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|D Chain D, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|E Chain E, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|F Chain F, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|G Chain G, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
pdb|4GTU|H Chain H, Ligand-Free Homodimeric Human Glutathione S-Transferase
M4- 4 (E.C.2.5.1.18)
Length = 217
Score = 26.9 bits (58), Expect = 5.1
Identities = 15/45 (33%), Positives = 26/45 (57%), Gaps = 10/45 (22%)
Query: 243 DNVQKLKYVVKMVAHLNGKTATFMPKPLYGDNGSGMHTHVSVWKN 287
D + + + + K+ A++ K++ F+PKPLY T V+VW N
Sbjct: 182 DFISRFEGLEKISAYM--KSSRFLPKPLY--------TRVAVWGN 216
>pdb|1AC4| Variation In The Strength Of A Ch To O Hydrogen Bond In An
Artificial Protein Cavity (2,3,4-Trimethyl-1,3-Thiazole)
pdb|1AC8| Variation In The Strength Of A Ch To O Hydrogen Bond In An
Artificial Protein Cavity (3,4,5-Trimethylthiazole)
pdb|1AEB| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase
(3-Methylthiazole)
pdb|1AED| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase
(3,4-Dimethylthiazole)
pdb|1AEE| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase (Aniline)
pdb|1AEF| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase (3-Aminopyridine)
pdb|1AEG| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase (4-Aminopyridine)
pdb|1AEH| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase
(2-Amino-4-Methylthiazole)
pdb|1AEJ| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase
(1-Vinylimidazole)
pdb|1AEK| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase (Indoline)
pdb|1AEM| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase
(Imidazo[1,2-A]pyridine)
pdb|1AEN| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase
(2-Amino-5-Methylthiazole)
pdb|1AEO| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase (2-Aminopyridine)
pdb|1AEQ| Variation In The Strength Of A Ch To O Hydrogen Bond In An
Artificial Protein Cavity (2-Ethylimidazole)
pdb|1AES| Specificity Of Ligand Binding To A Buried Polar Cavity At The
Active Site Of Cytochrome C Peroxidase (Imidazole)
pdb|1AET| Variation In The Strength Of A Ch To O Hydrogen Bond In An
Artificial Protein Cavity (1-Methylimidazole)
pdb|1AEU| Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C
Peroxidase (2-Methylimidazole)
pdb|1AEV| Introduction Of Novel Substrate Oxidation Into Cytochrome C
Peroxidase By Cavity Complementation: Oxidation Of
2-Aminothiazole And Covalent Modification Of The Enzyme
(2-Aminothiazole)
Length = 294
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 288
>pdb|1BEM| Interaction Between Proximal And Distals Regions Of Cytochrome C
Peroxidase
Length = 291
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 285
>pdb|1EBE|A Chain A, Laue Diffraction Study On The Structure Of Cytochrome C
Peroxidase Compound I
Length = 294
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 249 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 288
>pdb|1BEJ| Interaction Between Proximal And Distals Regions Of Cytochrome C
Peroxidase
Length = 291
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 285
>pdb|1BEK| Effect Of Unnatural Heme Substitution On Kinetics Of Electron
Transfer In Cytochrome C Peroxidase
Length = 291
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 285
>pdb|1BES| Interaction Between Proximal And Distals Regions Of Cytochrome C
Peroxidase
pdb|1BEQ| Interaction Between Proximal And Distals Regions Of Cytochrome C
Peroxidase
Length = 291
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 285
>pdb|1BEP| Effect Of Unnatural Heme Substitution On Kinetics Of Electron
Transfer In Cytochrome C Peroxidase
pdb|1BJ9| Effect Of Unnatural Heme Substitution On Kinetics Of Electron
Transfer In Cytochrome C Peroxidase
Length = 291
Score = 26.2 bits (56), Expect = 8.6
Identities = 13/41 (31%), Positives = 22/41 (52%), Gaps = 1/41 (2%)
Query: 437 KQYLKESQVFSEEFIQAYQSLKFNAEVFPWESKPHPFEFIT 477
K+Y + F ++F +A++ L + FP + P PF F T
Sbjct: 246 KEYANDQDKFFKDFSKAFEKLLEDGITFP-KDAPSPFIFKT 285
Database: /var/www/html/HP/blast_new/blast/db/pdbaa
Posted date: Dec 20, 2002 11:08 AM
Number of letters in database: 2,899,336
Number of sequences in database: 13,198
Lambda K H
0.319 0.137 0.406
Gapped
Lambda K H
0.267 0.0410 0.140
Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 2,941,404
Number of Sequences: 13198
Number of extensions: 129949
Number of successful extensions: 448
Number of sequences better than 10.0: 52
Number of HSP's better than 10.0 without gapping: 3
Number of HSP's successfully gapped in prelim test: 49
Number of HSP's that attempted gapping in prelim test: 432
Number of HSP's gapped (non-prelim): 52
length of query: 481
length of database: 2,899,336
effective HSP length: 92
effective length of query: 389
effective length of database: 1,685,120
effective search space: 655511680
effective search space used: 655511680
T: 11
A: 40
X1: 16 ( 7.4 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 41 (21.8 bits)
S2: 56 (26.2 bits)