1A71

TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE LIVER ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA WITH NAD AND TRIFLUOROETHANOL

Summary for 1A71

DescriptorLIVER ALCOHOL DEHYDROGENASE, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
Functional Keywordsoxidoreductase (nad(a)-choh(d)), liver, alcohol, dehydrogenase, ladh, active site mutant, oxidoreductase
Biological sourceEquus caballus (horse)
Cellular locationCytoplasm P00327
Total number of polymer chains2
Total molecular weight81517.08
Authors
Colby, T.D.,Bahnson, B.J.,Chin, J.K.,Klinman, J.P.,Goldstein, B.M. (deposition date: 1998-03-19, release date: 1998-06-17, Last modification date: 2011-07-13)
Primary citation
Colby, T.D.,Bahnson, B.J.,Chin, J.K.,Klinman, J.P.,Goldstein, B.M.
Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.
Biochemistry, 37:9295-9304, 1998
PubMed: 9649310 (PDB entries with the same primary citation)
DOI: 10.1021/bi973184b
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers70.3%2.3%0.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution