Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4CPA

REFINED CRYSTAL STRUCTURE OF THE POTATO INHIBITOR COMPLEX OF CARBOXYPEPTIDASE A AT 2.5 ANGSTROMS RESOLUTION

Replaces:  1CPA
Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
I0004857molecular_functionenzyme inhibitor activity
I0004866molecular_functionendopeptidase inhibitor activity
J0004857molecular_functionenzyme inhibitor activity
J0004866molecular_functionendopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN I 308
ChainResidue
AHIS69
AGLU72
AHIS196
IVAL38

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN J 309
ChainResidue
BHIS69
BGLU72
BHIS196
JVAL38

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GLY A 308
ChainResidue
AASN144
AARG145
AILE247
ATYR248
AGLU270
IVAL38
AHIS69

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GLY B 308
ChainResidue
BHIS69
BASN144
BARG145
BILE247
BTYR248
BGLU270
JVAL38

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 Residues586
DetailsDomain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12431056","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IY7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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_FI5
Number of Residues2
DetailsSite: {"description":"Interaction with carboxypeptidase"}
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

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon