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4IAV

G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris with N-Sulfamoyl-L-phenylalanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AHIS69
AGLU72
AHIS204
ACXA402

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CXA A 402
ChainResidue
AHIS204
ATHR205
ALEU211
AGLY251
ATYR255
AALA257
AGLU277
AZN401
AHOH660
AHIS69
AGLU72
AARG129
AASN146
AARG147

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
ASER7
ATYR9
AGLU14
AHOH570
AHOH676
AHOH755

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 404
ChainResidue
ATYR125
ASER223
ATYR288
AHOH595
AHOH625
AHOH711
AHOH768

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
ASER50
AASP51
AGLU57
AGLU59
AHOH587

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 406
ChainResidue
AASP56
AGLU57
AGLU61
AGLU104
AHOH685
AHOH686

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 407
ChainResidue
AARG183
AASN187
ATRP264
AGLN268
AHOH607
AHOH654

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 408
ChainResidue
AVAL16
AASN20
AASN25
ALYS32
ATRP45
AHOH548

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
AGLY193
ALYS194
AGLN195
AHIS269
AHOH596
AHOH637
AHOH751

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 410
ChainResidue
ALYS126
ASER127
ATRP128
ALYS152
AGLU166
AHOH635

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 411
ChainResidue
ASER34
AGLY36
ALYS37
AGLU43
AHOH593
AHOH790

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 412
ChainResidue
AHIS10
ALYS18
AHOH682

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 413
ChainResidue
ALYS48
ATYR106
AHOH575

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 414
ChainResidue
AGLY137
ASER138
ASER139
ATYR140
AARG171
ASER172
AHOH544
AHOH602

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 415
ChainResidue
APRO3
ASER4
ATYR5
AHOH681
AHOH743

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 416
ChainResidue
AGLU303
AHOH599
AHOH706

site_idBC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 417
ChainResidue
AHOH753
AHOH754
AHOH762
ATYR5
AASP291
AGLU292
AHOH591

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 418
ChainResidue
ATYR206
ASER207

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 419
ChainResidue
ASER139
ATYR140
AHOH787
AHOH788

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 420
ChainResidue
AASP51
AGLU57
AGLU59
AASN101
AHOH756
AHOH757

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PeVlYtaLhHArEhLTVemalyT
ChainResidueDetails
APRO60-THR82

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HTYSELIlYPY
ChainResidueDetails
AHIS204-TYR214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000305|PubMed:1521526
ChainResidueDetails
AGLU277

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:1521526
ChainResidueDetails
AHIS69
AGLU72
AHIS204

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PDB entries from 2024-06-12

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