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Structure paper

TitleActive site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.
Journal, issue, pagesBiochemistry, Vol. 37, Page 9295-9304, Year 1998
Publish dateMar 19, 1998 (structure data deposition date)
AuthorsColby, T.D. / Bahnson, B.J. / Chin, J.K. / Klinman, J.P. / Goldstein, B.M.
External linksBiochemistry / PubMed:9649310
MethodsX-ray diffraction
Resolution2 - 2.6 Å
Structure data

PDB-1a71:
TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE LIVER ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA WITH NAD AND TRIFLUOROETHANOL
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1a72:
AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD ANALOG CPAD
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

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

ChemComp-ETF:
TRIFLUOROETHANOL

ChemComp-HOH:
WATER

ChemComp-PAD:
5-BETA-D-RIBOFURANOSYLPICOLINAMIDE ADENINE-DINUCLEOTIDE

Source
  • equus caballus (horse)
KeywordsOXIDOREDUCTASE / OXIDOREDUCTASE (NAD(A)-CHOH(D)) / LIVER / ALCOHOL / DEHYDROGENASE / LADH / ACTIVE SITE MUTANT / LIVER ALCOHOL DEHYDROGENASE / ISOSTERIC NAD INHIBITORS

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