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1DTD

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
B0004857molecular_functionenzyme inhibitor activity
B0030414molecular_functionpeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AGLU300
AHIS424
AGLU427
AHIS552
BVAL66

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU A 300
ChainResidue
AARG482
AASN500
AARG501
AHIS552
ATYR604
AALA606
AGLU626
BVAL66
AHOH49
AHOH254
AZN301
AHIS424

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwLdaGiHArEwVTQatalwT
ChainResidueDetails
APRO415-THR437

site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLmFPY
ChainResidueDetails
AHIS552-TYR562

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Interaction with carboxypeptidase => ECO:0000250
ChainResidueDetails
BVAL66

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:10742178, ECO:0000269|PubMed:9384570
ChainResidueDetails
AARG426
AVAL429
AHIS552

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00730
ChainResidueDetails
ASER553
ATYR604
ATHR484
AASN500

218500

PDB entries from 2024-04-17

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