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4C5Y

Crystal structure of A. niger ochratoxinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005575cellular_componentcellular_component
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
A1900817biological_processochratoxin A catabolic process
B0004180molecular_functioncarboxypeptidase activity
B0005575cellular_componentcellular_component
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0046872molecular_functionmetal ion binding
B1900817biological_processochratoxin A catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AHIS111
AHIS113
AKCX246
AASP378
AZN501

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AZN500
AHIS111
AKCX246
AHIS287
AHIS307

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 500
ChainResidue
BHIS111
BHIS113
BKCX246
BASP378
BZN501

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BHIS111
BKCX246
BHIS287
BHIS307
BZN500

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:24947135
ChainResidueDetails
AKCX246
AASP378
BKCX246
BASP378

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:24947135, ECO:0007744|PDB:4C5Y
ChainResidueDetails
AHIS307
BHIS111
BHIS113
BKCX246
BHIS287
BHIS307
AHIS111
AHIS113
AKCX246
AHIS287

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PDB entries from 2024-06-12

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