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7CPA

COMPARISON OF THE STRUCTURES OF THREE CARBOXYPEPTIDASE A-PHOSPHONATE COMPLEXES DETERMINED BY X-RAY CRYSTALLOGRAPHY

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 308
ChainResidue
AHIS69
AGLU72
AHIS196
AFVF309

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FVF A 309
ChainResidue
AARG127
AASN144
AARG145
AHIS196
ASER197
ATYR198
AILE243
ATYR248
AALA250
AGLU270
APHE279
AZN308
AHOH311
AHOH343
AHOH441
AHIS69
AARG71
AGLU72

site_idFVF
Number of Residues1
Details
ChainResidue
AFVF309

site_idZN
Number of Residues1
Details
ChainResidue
AZN308

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 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:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7
ChainResidueDetails
AHIS69
AGLU72
AHIS196

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7
ChainResidueDetails
AARG127
AASN144
ASER197
ATYR248

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_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 2024-05-01

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