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Structure paper

TitleHistidine-51 facilitates deprotonatation of the zinc-bound ligand during catalysis by horse liver alcohol dehydrogenase
Journal, issue, pagesTo Be Published
Publish dateFeb 8, 2023 (structure data deposition date)
AuthorsPlapp, B.V.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.5 Å
Structure data

PDB-8g41:
Horse liver alcohol dehydrogense His-51-Gln form complexed with NADH
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

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

ChemComp-HOH:
WATER

Source
  • equus caballus (horse)
KeywordsOXIDOREDUCTASE / alcohol dehydrogenase horse liver His-51-Gln substitution complex with NADH

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