1b15: Difference between revisions
New page: left|200px<br /> <applet load="1b15" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b15, resolution 2.2Å" /> '''ALCOHOL DEHYDROGENAS... |
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==About this Structure== | ==About this Structure== | ||
1B15 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Scaptodrosophila_lebanonensis Scaptodrosophila lebanonensis]] with NAE as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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=1B15 OCA]]. | 1B15 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Scaptodrosophila_lebanonensis Scaptodrosophila lebanonensis]] with NAE as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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: ACA, ACB, CAA, CAB, NA1, NA2, NA3, NB1, NB2 and NB3. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B15 OCA]]. | ||
==Reference== | ==Reference== | ||
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., Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R, J Mol Biol. 1999 Jun 4;289(2):335-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10366509 10366509] | 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., Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R, J Mol Biol. 1999 Jun 4;289(2):335-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10366509 10366509] | ||
[[Category: Alcohol dehydrogenase]] | |||
[[Category: Scaptodrosophila lebanonensis]] | [[Category: Scaptodrosophila lebanonensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ternary complex]] | [[Category: ternary complex]] | ||
''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 13:05:28 2007'' | ||
Revision as of 14:00, 30 October 2007
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ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS TERNARY COMPLEX WITH NAD-ACETONE
OverviewOverview
Drosophila alcohol dehydrogenase (DADH) is an NAD+-dependent enzyme that, catalyzes the oxidation of alcohols to aldehydes/ketones. DADH is the, member of the short-chain dehydrogenases/reductases family (SDR) for which, the largest amount of biochemical data has been gathered during the last, three decades. The crystal structures of one binary form (NAD+) and three, ternary complexes with NAD+.acetone, NAD+.3-pentanone and, NAD+.cyclohexanone were solved at 2.4, 2.2, 1. 4 and 1.6 A resolution, respectively. From the molecular interactions observed, the reaction, mechanism could be inferred. The structure of DADH undergoes a, conformational change in order to bind the coenzyme. Furthermore, upon, binding of the ketone, a region that was disordered in the apo form, (186-191) gets ... [(full description)]
About this StructureAbout this Structure
1B15 is a [Single protein] structure of sequence from [Scaptodrosophila lebanonensis] with NAE 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 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., Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R, J Mol Biol. 1999 Jun 4;289(2):335-55. PMID:10366509
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