1B15
ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-ACETONE
Summary for 1B15
Entry DOI | 10.2210/pdb1b15/pdb |
Related | 1B14 1B2L |
Descriptor | ALCOHOL DEHYDROGENASE, NICOTINAMIDE ADENINE DINUCLEOTIDE ACETONE ADDUCT (3 entities in total) |
Functional Keywords | oxidoreductase, detoxification, metabolism, alcohol dehydrogenase, drosophila lebanonensis, short-chain dehydrogenases/reductases, ternary complex, nad- acetone adduct |
Biological source | Scaptodrosophila lebanonensis |
Total number of polymer chains | 2 |
Total formula weight | 57086.92 |
Authors | Benach, J.,Atrian, S.,Gonzalez-Duarte, R.,Ladenstein, R. (deposition date: 1998-11-25, release date: 1999-11-26, 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 (2.2 Å) |
Structure validation
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