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1PCA

THREE DIMENSIONAL STRUCTURE OF PORCINE PANCREATIC PROCARBOXYPEPTIDASE A. A COMPARISON OF THE A AND B ZYMOGENS AND THEIR DETERMINANTS FOR INHIBITION AND ACTIVATION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AHIS69
AGLU72
AHIS196
AHOH701

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT A 600
ChainResidue
ALYS224
ASER225
AHOH890
AASP19
AALA21
AGLN22
AHIS71
AGLN221

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE VAL A 700
ChainResidue
AARG127
AASN144
AARG145
ATYR248
AALA250
AGLU270
AHOH701

Functional Information from PROSITE/UniProt
site_idPS00132
Number of Residues23
DetailsCARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdsGiHSrEwITQasgvwF
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 Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379
ChainResidueDetails
AGLU270

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0007744|PDB:1PCA
ChainResidueDetails
AHIS69
AGLU72
AHIS196

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00730
ChainResidueDetails
AARG127
AASN144
ASER197
ATYR248

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG71
AGLU270
AARG127

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PDB entries from 2024-09-11

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