1A72

AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD ANALOG CPAD

Summary for 1A72

DescriptorHORSE LIVER ALCOHOL DEHYDROGENASE, ZINC ION, 5-BETA-D-RIBOFURANOSYLPICOLINAMIDE ADENINE-DINUCLEOTIDE, ... (4 entities in total)
Functional Keywordsoxidoreductase (nad(a)-choh(d)), active site mutant, liver alcohol dehydrogenase, isosteric nad inhibitors, oxidoreductase
Biological sourceEquus caballus (horse)
Cellular locationCytoplasm P00327
Total number of polymer chains1
Total molecular weight40658.5
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 (2.6 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers222.4%8.8%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution