1B16
ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-3-PENTANONE
Summary for 1B16
Entry DOI | 10.2210/pdb1b16/pdb |
Descriptor | PROTEIN (ALCOHOL DEHYDROGENASE), NICOTINAMIDE ADENINE DINUCLEOTIDE 3-PENTANONE ADDUCT (3 entities in total) |
Functional Keywords | oxidoreductase, detoxification, metabolism, alcohol dehydrogenase, drosophila lebanonensis, short-chain dehydrogenases/reductases, ternary complex, nad-3- pentanone adduct |
Biological source | Scaptodrosophila lebanonensis |
Total number of polymer chains | 2 |
Total formula weight | 57143.03 |
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 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 Cited by PubMed: 10366509DOI: 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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