1B2L

ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS: TERNARY COMPLEX WITH NAD-CYCLOHEXANONE

Summary for 1B2L

Related1B15 1B14
DescriptorALCOHOL DEHYDROGENASE, CALCIUM ION, NICOTINAMIDE ADENINE DINUCLEOTIDE CYCLOHEXANONE, ... (6 entities in total)
Functional Keywordsoxidoreductase, detoxification, metabolism, alcohol dehydrogenase, drosophila lebanonensis, short-chain dehydrogenases/reductases, ternary complex, nad- cyclohexanone adduct
Biological sourceScaptodrosophila lebanonensis
Total number of polymer chains1
Total molecular weight28876
Authors
Benach, J.,Atrian, S.,Gonzalez-Duarte, R.,Ladenstein, R. (deposition date: 1998-11-26, release date: 1999-11-26, Last modification date: 2018-03-07)
Primary citation
Benach, J.,Atrian, S.,Gonzalez-Duarte, R.,Ladenstein, R.
The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
J.Mol.Biol., 289:335-355, 1999
PubMed: 10366509 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1999.2765
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.6 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers20.4%1.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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