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TitleSubstitutions in the Flexible Loop of Horse Liver Alcohol Dehydrogenase Hinder the Conformational Change and Unmask Hydrogen Transfer
Journal, issue, pagesBiochemistry, Vol. 38, Page 13951-, Year 1999
Publish dateAug 31, 1999 (structure data deposition date)
AuthorsRamaswamy, S. / Park, D.H. / Plapp, B.V.
External linksBiochemistry / PubMed:10529241
MethodsX-ray diffraction
Resolution2.07 - 2.8 Å
Structure data

PDB-1qlh:
HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

PDB-1qlj:
HORSE LIVER ALCOHOL DEHYDROGENASE APO ENZYME DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-HOH:
WATER

Source
  • equus caballus (horse)
KeywordsOXIDOREDUCTASE / DEHYDROGENASE / ALCOHOL / NICOTINAMIDE COENZYME / DOUBLE MUTANT

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