1e3e
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(New page: 200px<br /> <applet load="1e3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e3e, resolution 2.12Å" /> '''MOUSE CLASS II ALCO...)
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Revision as of 19:55, 29 October 2007
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MOUSE CLASS II ALCOHOL DEHYDROGENASE COMPLEX WITH NADH
Overview
The structure of mouse class II alcohol dehydrogenase (ADH2) has been, determined in a binary complex with the coenzyme NADH and in a ternary, complex with both NADH and the inhibitor N-cyclohexylformamide to 2.2 A, and 2.1 A resolution, respectively. The ADH2 dimer is asymmetric in the, crystal with different orientations of the catalytic domains relative to, the coenzyme-binding domains in the two subunits, resulting in a slightly, different closure of the active-site cleft. Both conformations are about, half way between the open apo structure and the closed holo structure of, horse ADH1, thus resembling that of ADH3. The semi-open conformation and, structural differences around the active-site cleft contribute to a, substantially different substrate-binding pocket architecture as ... [(full description)]
About this Structure
1E3E is a [Single protein] structure of sequence from [Mus musculus] with ZN and NAD as [ligands]. Active as [[1]], with EC number [1.1.1.1]. Full crystallographic information is available from [OCA].
Reference
Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency., Svensson S, Hoog JO, Schneider G, Sandalova T, J Mol Biol. 2000 Sep 15;302(2):441-53. PMID:10970744
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