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2ABZ

Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
C0004857molecular_functionenzyme inhibitor activity
C0030414molecular_functionpeptidase inhibitor activity
D0004857molecular_functionenzyme inhibitor activity
D0030414molecular_functionpeptidase inhibitor activity
E0004857molecular_functionenzyme inhibitor activity
E0030414molecular_functionpeptidase inhibitor activity
F0004857molecular_functionenzyme inhibitor activity
F0030414molecular_functionpeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS69
AGLU72
AHIS196
CVAL66

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1002
ChainResidue
BHIS69
BGLU72
BHIS196
EVAL66

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF
ChainResidueDetails
APRO60-PHE82

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY
ChainResidueDetails
AHIS196-TYR206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Interaction with carboxypeptidase","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG127
AGLU270

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG127
BGLU270

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG71
AGLU270
AARG127

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG71
BGLU270
BARG127

site_idMCSA1
Number of Residues5
DetailsM-CSA 171
ChainResidueDetails
AHIS69metal ligand
AGLU72metal ligand
AARG127electrostatic stabiliser, hydrogen bond donor
AHIS196metal ligand
AGLU270covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 171
ChainResidueDetails
BHIS69metal ligand
BGLU72metal ligand
BARG127electrostatic stabiliser, hydrogen bond donor
BHIS196metal ligand
BGLU270covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor

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PDB entries from 2025-12-24

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