1e3e
From Proteopedia
(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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==About this Structure== | ==About this Structure== | ||
| - | 1E3E is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with ZN and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3E OCA]]. | + | 1E3E is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with ZN and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1]]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5 and AC6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3E OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10970744 10970744] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10970744 10970744] | ||
| + | [[Category: Alcohol dehydrogenase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alcohol dehydrogenase]] | [[Category: alcohol dehydrogenase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:25:53 2007'' |
Revision as of 12:21, 30 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 [Alcohol dehydrogenase], with EC number [1.1.1.1]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5 and AC6. 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
Page seeded by OCA on Tue Oct 30 14:25:53 2007
