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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 Residues4
DetailsSITE: Interaction with carboxypeptidase => ECO:0000250
ChainResidueDetails
CVAL66
DVAL66
EVAL66
FVAL66

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7
ChainResidueDetails
AHIS69
AGLU72
AHIS196
BHIS69
BGLU72
BHIS196

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7
ChainResidueDetails
AARG127
AASN144
ASER197
ATYR248
BARG127
BASN144
BSER197
BTYR248

Catalytic Information from CSA
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 2024-04-24

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