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4IK2

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AHIS69
AARG129
AASN146
AARG147
ATYR255
AGLU277
ABL2403

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
AHIS204
ABL2403
AHIS69
AGLU72

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BL2 A 403
ChainResidue
AHIS69
AARG71
AGLU72
AARG129
AHIS204
ATHR205
ATYR206
ASER207
ATYR255
AGLU277
APHE287
ASO4401
AZN402
AHOH519

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ASER50
AASP51
AGLU57
AGLU59
AHOH709

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
AASP56
AGLU57
AGLU61
AGLU104
AHOH710
AHOH737

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 406
ChainResidue
AASP51
AGLU57
AGLU59
AASN101

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 407
ChainResidue
ASER7
ATYR9
AGLU14
AHOH640
AHOH678
AHOH826

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 2024-08-21

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