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; PubMed: 10366509; DOI: 10.1006/jmbi.1999.2765

Experimental method

X-RAY DIFFRACTION (2.2 Å)