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3VXG

Crystal structure of conjugated polyketone reductase C2 from Candida Parapsilosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005575cellular_componentcellular_component
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016652molecular_functionoxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor
A0036441molecular_function2-dehydropantolactone reductase activity
A0042180biological_processcellular ketone metabolic process
A0044281biological_processsmall molecule 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
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:23828603
ChainResidueDetails
AHIS125
ATYR63

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:23828603, ECO:0007744|PDB:4H8N
ChainResidueDetails
ALYS28
AASP58
ASER161
AGLN186
ASER215
ALEU217
AARG222
ATHR260
ATHR261
ASER262
ASER263
ALYS264
AARG267
ATHR27
AGLY26

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000305|PubMed:23828603
ChainResidueDetails
ALYS88

221051

PDB entries from 2024-06-12

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