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1b14
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(New page: 200px<br /> <applet load="1b14" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b14, resolution 2.4Å" /> '''ALCOHOL DEHYDROGENAS...)
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Revision as of 18:04, 29 October 2007
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ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS BINARY COMPLEX WITH NAD+
Overview
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 Structure
1B14 is a [Single protein] structure of sequence from [Scaptodrosophila lebanonensis] with NAD as [ligand]. Active as [[1]], with EC number [1.1.1.1]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 20:08:58 2007
