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1B16

ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-3-PENTANONE

Summary for 1B16
Entry DOI10.2210/pdb1b16/pdb
DescriptorPROTEIN (ALCOHOL DEHYDROGENASE), NICOTINAMIDE ADENINE DINUCLEOTIDE 3-PENTANONE ADDUCT (3 entities in total)
Functional Keywordsoxidoreductase, detoxification, metabolism, alcohol dehydrogenase, drosophila lebanonensis, short-chain dehydrogenases/reductases, ternary complex, nad-3- pentanone adduct
Biological sourceScaptodrosophila lebanonensis
Total number of polymer chains2
Total formula weight57143.03
Authors
Benach, J.,Atrian, S.,Gonzalez-Duarte, R.,Ladenstein, R. (deposition date: 1998-11-25, release date: 1999-11-29, Last modification date: 2023-08-09)
Primary citationBenach, 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
Cited by
PubMed: 10366509
DOI: 10.1006/jmbi.1999.2765
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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