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3VXG

Crystal structure of conjugated polyketone reductase C2 from Candida Parapsilosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0016491molecular_functionoxidoreductase activity
A0016652molecular_functionoxidoreductase activity, acting on NAD(P)H as acceptor
A0036441molecular_function2-dehydropantolactone reductase activity
A0042180biological_processketone metabolic process
A0047011molecular_function2-dehydropantolactone reductase (A-specific) activity
Functional Information from PROSITE/UniProt
site_idPS00422
Number of Residues10
DetailsGRANINS_1 Granins signature 1. ESLNLFDfEL
ChainResidueDetails
AGLU270-LEU279

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GFRHIDTAeayntQkeVG
ChainResidueDetails
AGLY53-GLY70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23828603","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23828603","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4H8N","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"PubMed","id":"23828603","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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