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7E6O

Crystal structure of polyol dehydrogenase from Paracoccus denitrificans

Functional Information from GO Data
ChainGOidnamespacecontents
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0048038molecular_functionquinone binding
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0048038molecular_functionquinone binding
C0006633biological_processfatty acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0048038molecular_functionquinone binding
D0006633biological_processfatty acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0048038molecular_functionquinone binding
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SqagrrgeplVavYCASKAAViSMTqSAG
ChainResidueDetails
CSER139-GLY167

246905

PDB entries from 2025-12-31

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