1b14: Difference between revisions
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[[Category: short-chain dehydrogenases/reductases]] | [[Category: short-chain dehydrogenases/reductases]] | ||
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Revision as of 15:48, 30 October 2007
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ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS BINARY COMPLEX WITH NAD+
OverviewOverview
Drosophila alcohol dehydrogenase (DADH; EC 1.1.1.1) is a NAD(H)-dependent, oxidoreductase belonging to the short-chain dehydrogenases/reductases, (SDR) family. This homodimeric enzyme catalyzes the dehydrogenation of, alcohols to their respective ketones or aldehydes in the fruit-fly, Drosophila, both for metabolic assimilation and detoxification purposes., The crystal structure of the apo form of DADH, one of the first, biochemically characterized member of the SDR family, was solved at 1.9 A, resolution by Patterson methods. The initial model was improved by, crystallographic refinement accompanied by electron density averaging, R-factor=20.5%, R-free=23.8%.DADH subunits show an alpha/beta single, domain structure with a characteristic NAD(H) binding motif (Rossmann, fold). The peptide ... [(full description)]
About this StructureAbout this Structure
1B14 is a [Single protein] structure of sequence from [Scaptodrosophila lebanonensis] with NAD as [ligand]. Active as [Alcohol dehydrogenase], with EC number [1.1.1.1]. Structure known Active Sites: ACA, ACB, CAA, CAB, NA1, NA2, NA3, NB1, NB2 and NB3. Full crystallographic information is available from [OCA].
ReferenceReference
The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution., Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R, J Mol Biol. 1998 Sep 18;282(2):383-99. PMID:9735295
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