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|15645851|ref|NP_208029.1| carbamoyl-phosphate
synthetase (pyrAa) [Helicobacter pylori 26695]
(375 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|1JDB|F Chain F, Carbamoyl Phosphate Synthetase From Esc... 256 4e-69
pdb|1C30|B Chain B, Crystal Structure Of Carbamoyl Phosphat... 253 3e-68
pdb|1CS0|B Chain B, Crystal Structure Of Carbamoyl Phosphat... 252 4e-68
pdb|1M6V|B Chain B, Crystal Structure Of The G359f (Small S... 252 4e-68
pdb|1A9X|B Chain B, Carbamoyl Phosphate Synthetase: Caught ... 249 5e-67
pdb|1QDL|B Chain B, The Crystal Structure Of Anthranilate S... 63 5e-11
pdb|1I1Q|B Chain B, Structure Of The Cooperative Allosteric... 50 3e-07
pdb|1I7Q|B Chain B, Anthranilate Synthase From S. Marcescen... 50 5e-07
pdb|1L9X|B Chain B, Structure Of Gamma-Glutamyl Hydrolase >... 30 0.44
pdb|1GPM|A Chain A, Escherichia Coli Gmp Synthetase Complex... 29 0.99
pdb|1EE3|P Chain P, Cadmium-Substituted Bovine Pancreatic C... 26 8.4
pdb|1CBX| Carboxypeptidase A (E.C.3.4.17.1) Complex With ... 26 8.4
pdb|2CTC| Carboxypeptidase A (E.C.3.4.17.1) Complex With ... 26 8.4
pdb|1PYT|B Chain B, Ternary Complex Of Procarboxypeptidase ... 26 8.4
pdb|1F57|A Chain A, Carboxypeptidase A Complex With D-Cyste... 26 8.4
>pdb|1JDB|F Chain F, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1JDB|C Chain C, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1JDB|I Chain I, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1JDB|L Chain L, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1CE8|B Chain B, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1CE8|D Chain D, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1CE8|F Chain F, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1CE8|H Chain H, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1BXR|B Chain B, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
pdb|1BXR|D Chain D, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
pdb|1BXR|F Chain F, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
pdb|1BXR|H Chain H, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
Length = 382
Score = 256 bits (653), Expect = 4e-69
Identities = 146/377 (38%), Positives = 210/377 (54%), Gaps = 11/377 (2%)
Query: 4 LYLENGLFLQAQSFGASGTQAGELVFNTSMSGYQEVISDPSYKGQFVVFSMPEIGVVGAN 63
L LE+G ++ GA+G+ GE+VFNTSM+GYQE+++DPSY Q V + P IG VG N
Sbjct: 7 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTN 66
Query: 64 SKDDESF-FSCAGVLARHYNEFFSNSRADFSLSAYLKERGVLGVCGVDTRSLIKTLRHHG 122
D+ES G++ R SN R LS+YLK ++ + +DTR L + LR G
Sbjct: 67 DADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKG 126
Query: 123 CLM-MVASTIEHDKNKLEEILKNAPKISHSPLVSSVSTPKITTHQRATFDFK--TLDYKP 179
+ + D E + P ++ L V+T + + + ++ K
Sbjct: 127 AQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPQAKK 186
Query: 180 FDEKTSHKIIAVLDFGAKGNILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSN 239
DE H + DFGAK NIL L + G + I P T A +++K GIFLSN
Sbjct: 187 EDELPFH--VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNP----DGIFLSN 240
Query: 240 GPGDPLSLQQEIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKNL 299
GPGDP I I++ + IP+ GICLGHQLL++A G T K+KFGHHG NHPVK++
Sbjct: 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDV 300
Query: 300 KTNAVEITAQNHNYCVPE-DIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPESSPGP 358
+ N V ITAQNH + V E + +TH++LFD T++G+ + P S Q HPE+SPGP
Sbjct: 301 EKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGP 360
Query: 359 KESHYIFKEFVELLKDF 375
++ +F F+EL++ +
Sbjct: 361 HDAAPLFDHFIELIEQY 377
>pdb|1C30|B Chain B, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C30|D Chain D, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C30|F Chain F, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C30|H Chain H, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C3O|B Chain B, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
pdb|1C3O|D Chain D, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
pdb|1C3O|F Chain F, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
pdb|1C3O|H Chain H, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
Length = 382
Score = 253 bits (645), Expect = 3e-68
Identities = 145/377 (38%), Positives = 210/377 (55%), Gaps = 11/377 (2%)
Query: 4 LYLENGLFLQAQSFGASGTQAGELVFNTSMSGYQEVISDPSYKGQFVVFSMPEIGVVGAN 63
L LE+G ++ GA+G+ GE+VFNTSM+GYQE+++DPSY Q V + P IG VG N
Sbjct: 7 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTN 66
Query: 64 SKDDESF-FSCAGVLARHYNEFFSNSRADFSLSAYLKERGVLGVCGVDTRSLIKTLRHHG 122
D+ES G++ R SN R LS+YLK ++ + +DTR L + LR G
Sbjct: 67 DADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKG 126
Query: 123 CLM-MVASTIEHDKNKLEEILKNAPKISHSPLVSSVSTPKITTHQRATFDFK--TLDYKP 179
+ + D E + P ++ L V+T + + + ++ + K
Sbjct: 127 AQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPEAKK 186
Query: 180 FDEKTSHKIIAVLDFGAKGNILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSN 239
DE H + DFGAK NIL L + G + I P T A +++K GIFLSN
Sbjct: 187 EDELPFH--VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNP----DGIFLSN 240
Query: 240 GPGDPLSLQQEIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKNL 299
GPGDP I I++ + IP+ GI LGHQLL++A G T K+KFGHHG NHPVK++
Sbjct: 241 GPGDPAPCDYAITAIQKFLETDIPVFGISLGHQLLALASGAKTVKMKFGHHGGNHPVKDV 300
Query: 300 KTNAVEITAQNHNYCVPE-DIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPESSPGP 358
+ N V ITAQNH + V E + +TH++LFD T++G+ + P S Q HPE+SPGP
Sbjct: 301 EKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGP 360
Query: 359 KESHYIFKEFVELLKDF 375
++ +F F+EL++ +
Sbjct: 361 HDAAPLFDHFIELIEQY 377
>pdb|1CS0|B Chain B, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1CS0|D Chain D, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1CS0|F Chain F, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1CS0|H Chain H, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1KEE|B Chain B, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
pdb|1KEE|D Chain D, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
pdb|1KEE|F Chain F, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
pdb|1KEE|H Chain H, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
Length = 382
Score = 252 bits (644), Expect = 4e-68
Identities = 145/377 (38%), Positives = 210/377 (55%), Gaps = 11/377 (2%)
Query: 4 LYLENGLFLQAQSFGASGTQAGELVFNTSMSGYQEVISDPSYKGQFVVFSMPEIGVVGAN 63
L LE+G ++ GA+G+ GE+VFNTSM+GYQE+++DPSY Q V + P IG VG N
Sbjct: 7 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTN 66
Query: 64 SKDDESF-FSCAGVLARHYNEFFSNSRADFSLSAYLKERGVLGVCGVDTRSLIKTLRHHG 122
D+ES G++ R SN R LS+YLK ++ + +DTR L + LR G
Sbjct: 67 DADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKG 126
Query: 123 CLM-MVASTIEHDKNKLEEILKNAPKISHSPLVSSVSTPKITTHQRATFDFK--TLDYKP 179
+ + D E + P ++ L V+T + + + ++ + K
Sbjct: 127 AQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPEAKK 186
Query: 180 FDEKTSHKIIAVLDFGAKGNILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSN 239
DE H + DFGAK NIL L + G + I P T A +++K GIFLSN
Sbjct: 187 EDELPFH--VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNP----DGIFLSN 240
Query: 240 GPGDPLSLQQEIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKNL 299
GPGDP I I++ + IP+ GI LGHQLL++A G T K+KFGHHG NHPVK++
Sbjct: 241 GPGDPAPCDYAITAIQKFLETDIPVFGIXLGHQLLALASGAKTVKMKFGHHGGNHPVKDV 300
Query: 300 KTNAVEITAQNHNYCVPE-DIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPESSPGP 358
+ N V ITAQNH + V E + +TH++LFD T++G+ + P S Q HPE+SPGP
Sbjct: 301 EKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPGP 360
Query: 359 KESHYIFKEFVELLKDF 375
++ +F F+EL++ +
Sbjct: 361 HDAAPLFDHFIELIEQY 377
>pdb|1M6V|B Chain B, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
pdb|1M6V|D Chain D, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
pdb|1M6V|F Chain F, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
pdb|1M6V|H Chain H, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
Length = 382
Score = 252 bits (644), Expect = 4e-68
Identities = 145/377 (38%), Positives = 209/377 (54%), Gaps = 11/377 (2%)
Query: 4 LYLENGLFLQAQSFGASGTQAGELVFNTSMSGYQEVISDPSYKGQFVVFSMPEIGVVGAN 63
L LE+G ++ GA+G+ GE+VFNTSM+GYQE+++DPSY Q V + P IG VG N
Sbjct: 7 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTN 66
Query: 64 SKDDESF-FSCAGVLARHYNEFFSNSRADFSLSAYLKERGVLGVCGVDTRSLIKTLRHHG 122
D+ES G++ R SN R LS+YLK ++ + +DTR L + LR G
Sbjct: 67 DADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKG 126
Query: 123 CLM-MVASTIEHDKNKLEEILKNAPKISHSPLVSSVSTPKITTHQRATFDFK--TLDYKP 179
+ + D E + P ++ L V+T + + + ++ K
Sbjct: 127 AQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPQAKK 186
Query: 180 FDEKTSHKIIAVLDFGAKGNILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSN 239
DE H + DFGAK NIL L + G + I P T A +++K GIFLSN
Sbjct: 187 EDELPFH--VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNP----DGIFLSN 240
Query: 240 GPGDPLSLQQEIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKNL 299
GPGDP I I++ + IP+ GICLGHQLL++A G T K+KFGHHG NHPVK++
Sbjct: 241 GPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNHPVKDV 300
Query: 300 KTNAVEITAQNHNYCVPE-DIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPESSPGP 358
+ N V ITAQNH + V E + +TH++LFD T++G+ + P S Q HPE+SP P
Sbjct: 301 EKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGHPEASPFP 360
Query: 359 KESHYIFKEFVELLKDF 375
++ +F F+EL++ +
Sbjct: 361 HDAAPLFDHFIELIEQY 377
>pdb|1A9X|B Chain B, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
pdb|1A9X|D Chain D, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
pdb|1A9X|F Chain F, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
pdb|1A9X|H Chain H, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
Length = 379
Score = 249 bits (635), Expect = 5e-67
Identities = 144/377 (38%), Positives = 209/377 (55%), Gaps = 11/377 (2%)
Query: 4 LYLENGLFLQAQSFGASGTQAGELVFNTSMSGYQEVISDPSYKGQFVVFSMPEIGVVGAN 63
L LE+G ++ GA+G+ GE+VFNTSM+GYQE+++DPSY Q V + P IG VG N
Sbjct: 6 LVLEDGTQFHGRAIGATGSAVGEVVFNTSMTGYQEILTDPSYSRQIVTLTYPHIGNVGTN 65
Query: 64 SKDDESF-FSCAGVLARHYNEFFSNSRADFSLSAYLKERGVLGVCGVDTRSLIKTLRHHG 122
D+ES G++ R SN R LS+YLK ++ + +DTR L + LR G
Sbjct: 66 DADEESSQVHAQGLVIRDLPLIASNFRNTEDLSSYLKRHNIVAIADIDTRKLTRLLREKG 125
Query: 123 CLM-MVASTIEHDKNKLEEILKNAPKISHSPLVSSVSTPKITTHQRATFDFK--TLDYKP 179
+ + D E + P ++ L V+T + + + ++ K
Sbjct: 126 AQNGCIIAGDNPDAALALEKARAFPGLNGMDLAKEVTTAEAYSWTQGSWTLTGGLPQAKK 185
Query: 180 FDEKTSHKIIAVLDFGAKGNILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSN 239
DE H + DFGAK NIL L + G + I P T A +++K GIFLSN
Sbjct: 186 EDELPFH--VVAYDFGAKRNILRMLVDRGCRLTIVPAQTSAEDVLKMNP----DGIFLSN 239
Query: 240 GPGDPLSLQQEIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKNL 299
GPGDP I I++ + IP+ GI LGHQLL++A G T K+KFGHHG NHPVK++
Sbjct: 240 GPGDPAPCDYAITAIQKFLETDIPVFGIXLGHQLLALASGAKTVKMKFGHHGGNHPVKDV 299
Query: 300 KTNAVEITAQNHNYCVPE-DIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPESSPGP 358
+ N V ITAQNH + V E + +TH++LFD T++G+ + P S Q +PE+SPGP
Sbjct: 300 EKNVVMITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAFSFQGNPEASPGP 359
Query: 359 KESHYIFKEFVELLKDF 375
++ +F F+EL++ +
Sbjct: 360 HDAAPLFDHFIELIEQY 376
>pdb|1QDL|B Chain B, The Crystal Structure Of Anthranilate Synthase From
Sulfolobus Solfataricus
Length = 195
Score = 63.2 bits (152), Expect = 5e-11
Identities = 43/153 (28%), Positives = 74/153 (48%), Gaps = 13/153 (8%)
Query: 214 YPHHTKASEL-IKAYEKKEISGIFLSNGPGDPLSLQQEIG---EIKQLINAKIPMLGICL 269
YP + E+ IK E+ + + +S GPG P +++IG ++ + + + P+LG+CL
Sbjct: 27 YPIVIRNDEISIKGIERIDPDRLIISPGPGTP-EKREDIGVSLDVIKYLGKRTPILGVCL 85
Query: 270 GHQLLSIAQGYPTYKLKFGHHG--------SNHPVKNLKTNAVEITAQNHNYCVPEDIEE 321
GHQ + A G + + HG +N P+ A E A ++ V +++
Sbjct: 86 GHQAIGYAFGAKIRRARKVFHGKISNIILVNNSPLSLYYGIAKEFKATRYHSLVVDEVHR 145
Query: 322 IAIITHRNLFDNTIEGVRYKNAPIISVQHHPES 354
I+ + DN I + ++ PI VQ HPES
Sbjct: 146 PLIVDAISAEDNEIMAIHHEEYPIYGVQFHPES 178
>pdb|1I1Q|B Chain B, Structure Of The Cooperative Allosteric Anthranilate
Synthase From Salmonella Typhimurium
Length = 192
Score = 50.4 bits (119), Expect = 3e-07
Identities = 45/166 (27%), Positives = 75/166 (45%), Gaps = 18/166 (10%)
Query: 199 NILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSNGPGDPLSLQQEIGEIKQLI 258
N+ ++L+ G +IY +H A LI + + LS GPG P E G + +L+
Sbjct: 15 NLADQLRTNGHNVVIYRNHIPAQTLIDRLATMKNPVLMLSPGPGVP----SEAGCMPELL 70
Query: 259 N---AKIPMLGICLGHQLLSIAQGYPTYKLKFGH--HGSNHPVKN-----LKTNAVEITA 308
K+P++GICLGHQ +I + Y Y + G HG +++ A +
Sbjct: 71 TRLRGKLPIIGICLGHQ--AIVEAYGGYVGQAGEILHGKATSIEHDGQAMFAGLANPLPV 128
Query: 309 QNHNYCVPEDIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPES 354
++ V ++ A +T F+ + VR+ + Q HPES
Sbjct: 129 ARYHSLVGSNVP--AGLTINAHFNGMVMAVRHDADRVCGFQFHPES 172
>pdb|1I7Q|B Chain B, Anthranilate Synthase From S. Marcescens
pdb|1I7Q|D Chain D, Anthranilate Synthase From S. Marcescens
pdb|1I7S|B Chain B, Anthranilate Synthase From Serratia Marcescens In Complex
With Its End Product Inhibitor L-Tryptophan
pdb|1I7S|D Chain D, Anthranilate Synthase From Serratia Marcescens In Complex
With Its End Product Inhibitor L-Tryptophan
Length = 193
Score = 49.7 bits (117), Expect = 5e-07
Identities = 43/164 (26%), Positives = 72/164 (43%), Gaps = 14/164 (8%)
Query: 199 NILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSNGPGDPLSLQQEIG---EIK 255
N++++L+ G + +IY + A +I+ + E + LS GPG P E G E+
Sbjct: 16 NLVDQLRASGHQVVIYRNQIGAEVIIERLQHMEQPVLMLSPGPGTP----SEAGCMPELL 71
Query: 256 QLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHPVKN-----LKTNAVEITAQN 310
Q + ++P++GICLGHQ + A G + HG + + A +
Sbjct: 72 QRLRGQLPIIGICLGHQAIVEAYGGQVGQAGEILHGKASAIAHDGEGMFAGMANPLPVAR 131
Query: 311 HNYCVPEDIEEIAIITHRNLFDNTIEGVRYKNAPIISVQHHPES 354
++ V +I A +T F + VR + Q HPES
Sbjct: 132 YHSLVGSNIP--ADLTVNARFGEMVMAVRDDRRRVCGFQFHPES 173
>pdb|1L9X|B Chain B, Structure Of Gamma-Glutamyl Hydrolase
pdb|1L9X|D Chain D, Structure Of Gamma-Glutamyl Hydrolase
pdb|1L9X|A Chain A, Structure Of Gamma-Glutamyl Hydrolase
pdb|1L9X|C Chain C, Structure Of Gamma-Glutamyl Hydrolase
Length = 315
Score = 30.0 bits (66), Expect = 0.44
Identities = 24/77 (31%), Positives = 38/77 (49%), Gaps = 16/77 (20%)
Query: 293 NHPVKNLKTNAVE-ITAQNH-------NYCVPEDIEEIAIITHRNL-----FDNTIEGVR 339
N P + L + AVE +TA H N+ + E +++ + N F +T+EG +
Sbjct: 173 NFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYK 232
Query: 340 YKNAPIISVQHHPESSP 356
Y P+ VQ HPE +P
Sbjct: 233 Y---PVYGVQWHPEKAP 246
>pdb|1GPM|A Chain A, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
pdb|1GPM|C Chain C, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
pdb|1GPM|B Chain B, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
pdb|1GPM|D Chain D, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
Length = 525
Score = 28.9 bits (63), Expect = 0.99
Identities = 21/96 (21%), Positives = 47/96 (48%), Gaps = 8/96 (8%)
Query: 186 HKIIAVLDFGAKGN--ILNELQNVGLKALIYPHHTKASELIKAYEKKEISGIFLSNGPGD 243
H+I+ +LDFG++ + ++ +G+ ++ +++ SGI LS GP +
Sbjct: 8 HRIL-ILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQI----RDFNPSGIILSGGP-E 61
Query: 244 PLSLQQEIGEIKQLINAKIPMLGICLGHQLLSIAQG 279
+ + + + A +P+ G+C G Q +++ G
Sbjct: 62 STTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLG 97
>pdb|1EE3|P Chain P, Cadmium-Substituted Bovine Pancreatic Carboxypeptidase A
(Alfa-Form) At Ph 7.5 And 2 Mm Chloride In Monoclinic
Crystal Form
pdb|1ELL|P Chain P, Cadmium-Substituted Bovine Pancreatic Carboxypeptidase A
(Alfa-Form) At Ph 7.5 And 0.25 M Chloride In Monoclinic
Crystal Form.
pdb|1ELM|P Chain P, Cadmium-Substituted Bovine Pacreatic Carboxypeptidase A
(Alfa-Form) At Ph 5.5 And 2 Mm Chloride In Monoclinic
Crystal Form.
pdb|1YME| Structure Of Carboxypeptidase
pdb|1ARM| Carboxypeptidase A With Zn Replaced By Hg
Length = 309
Score = 25.8 bits (55), Expect = 8.4
Identities = 18/46 (39%), Positives = 23/46 (49%), Gaps = 2/46 (4%)
Query: 250 EIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHP 295
EI + L+ A+ P L L Q+ +G P Y LKF GSN P
Sbjct: 17 EIYDFMDLLVAEHPQLVSKL--QIGRSYEGRPIYVLKFSTGGSNRP 60
>pdb|1CBX| Carboxypeptidase A (E.C.3.4.17.1) Complex With L-Benzylsuccinate
Inhibitor
pdb|1CPS| Carboxypeptidase A (E.C.3.4.17.1) Complex With The Sulfodiimine
Inhibitor: Cpm,
[l-(-)-2-Carboxy-3-Phenylpropyl]methyl-Sulfodiimine
Length = 307
Score = 25.8 bits (55), Expect = 8.4
Identities = 18/46 (39%), Positives = 23/46 (49%), Gaps = 2/46 (4%)
Query: 250 EIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHP 295
EI + L+ A+ P L L Q+ +G P Y LKF GSN P
Sbjct: 17 EIYDFMDLLVAEHPQLVSKL--QIGRSYEGRPIYVLKFSTGGSNRP 60
>pdb|2CTC| Carboxypeptidase A (E.C.3.4.17.1) Complex With L-Phenyl Lactate
(L-O-Phe)
pdb|2CTB| Carboxypeptidase A (E.C.3.4.17.1)
pdb|1HDQ|A Chain A, Crystal Structure Of Bovine Pancreatic Carboxypeptidase A
Complexed With D-N-Hydroxyaminocarbonyl Phenylalanine At
2.3 A
Length = 307
Score = 25.8 bits (55), Expect = 8.4
Identities = 18/46 (39%), Positives = 23/46 (49%), Gaps = 2/46 (4%)
Query: 250 EIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHP 295
EI + L+ A+ P L L Q+ +G P Y LKF GSN P
Sbjct: 17 EIYDFMDLLVAEHPQLVSKL--QIGRSYEGRPIYVLKFSTGGSNRP 60
>pdb|1PYT|B Chain B, Ternary Complex Of Procarboxypeptidase A, Proproteinase E,
And Chymotrypsinogen C
Length = 309
Score = 25.8 bits (55), Expect = 8.4
Identities = 18/46 (39%), Positives = 23/46 (49%), Gaps = 2/46 (4%)
Query: 250 EIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHP 295
EI + L+ A+ P L L Q+ +G P Y LKF GSN P
Sbjct: 17 EIYDFMDLLVAEHPQLVSKL--QIGRSYEGRPIYVLKFSTGGSNRP 60
>pdb|1F57|A Chain A, Carboxypeptidase A Complex With D-Cysteine At 1.75 A
pdb|1ARL| Carboxypeptidase A With Zn Removed
pdb|1CPX|A Chain A, Beta Form Of Carboxypeptidase A (Residues 3-307) From
Bovine Pancreas In An Orthorhombic Crystal Form With Two
Zinc Ions In The Active Site
Length = 307
Score = 25.8 bits (55), Expect = 8.4
Identities = 18/46 (39%), Positives = 23/46 (49%), Gaps = 2/46 (4%)
Query: 250 EIGEIKQLINAKIPMLGICLGHQLLSIAQGYPTYKLKFGHHGSNHP 295
EI + L+ A+ P L L Q+ +G P Y LKF GSN P
Sbjct: 17 EIYDFMDLLVAEHPQLVSKL--QIGRSYEGRPIYVLKFSTGGSNRP 60
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
0.318 0.136 0.391
Gapped
Lambda K H
0.267 0.0410 0.140
Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 2,206,241
Number of Sequences: 13198
Number of extensions: 91783
Number of successful extensions: 290
Number of sequences better than 10.0: 15
Number of HSP's better than 10.0 without gapping: 8
Number of HSP's successfully gapped in prelim test: 7
Number of HSP's that attempted gapping in prelim test: 259
Number of HSP's gapped (non-prelim): 15
length of query: 375
length of database: 2,899,336
effective HSP length: 90
effective length of query: 285
effective length of database: 1,711,516
effective search space: 487782060
effective search space used: 487782060
T: 11
A: 40
X1: 16 ( 7.3 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 41 (21.7 bits)
S2: 55 (25.8 bits)