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TitleOrigins of the high catalytic activity of human alcohol dehydrogenase 4 studied with horse liver A317C alcohol dehydrogenase.
Journal, issue, pagesChem. Biol. Interact, Vol. 191, Page 42-47, Year 2011
Publish dateSep 2, 2010 (structure data deposition date)
AuthorsHerdendorf, T.J. / Plapp, B.V.
External linksChem. Biol. Interact / PubMed:21184752
MethodsX-ray diffraction
Resolution1.2 Å
Structure data

PDB-3oq6:
Horse liver alcohol dehydrogenase A317C mutant complexed with NAD+ and 2,3,4,5,6-pentafluorobenzyl alcohol
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAJ:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE (ACIDIC FORM)

ChemComp-PFB:
2,3,4,5,6-PENTAFLUOROBENZYL ALCOHOL

ChemComp-MRD:
(4R)-2-METHYLPENTANE-2,4-DIOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • equus caballus (horse)
KeywordsOXIDOREDUCTASE / Rossmann fold / alcohol metabolism / NAD

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