1e6w
From Proteopedia
(New page: 200px<br /> <applet load="1e6w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e6w, resolution 1.7Å" /> '''RAT BRAIN 3-HYDROXYA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1E6W is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with NAD and EST 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=1.1.1.35 1.1.1.35]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E6W OCA]]. | + | 1E6W is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with NAD and EST as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/3-hydroxyacyl-CoA_dehydrogenase 3-hydroxyacyl-CoA dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.35 1.1.1.35]]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, ASA, ASB, ASC and ASD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E6W OCA]]. |
==Reference== | ==Reference== | ||
Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD)., Powell AJ, Read JA, Banfield MJ, Gunn-Moore F, Yan SD, Lustbader J, Stern AR, Stern DM, Brady RL, J Mol Biol. 2000 Oct 20;303(2):311-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11023795 11023795] | Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD)., Powell AJ, Read JA, Banfield MJ, Gunn-Moore F, Yan SD, Lustbader J, Stern AR, Stern DM, Brady RL, J Mol Biol. 2000 Oct 20;303(2):311-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11023795 11023795] | ||
| + | [[Category: 3-hydroxyacyl-CoA dehydrogenase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: steroids]] | [[Category: steroids]] | ||
| - | ''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 12:40:05 2007'' |
Revision as of 10:35, 30 October 2007
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RAT BRAIN 3-HYDROXYACYL-COA DEHYDROGENASE BINARY COMPLEX WITH NADH AND ESTRADIOL
Overview
Human type II hydroxyacyl-CoA dehydrogenase/amyloid-beta binding alcohol, dehydrogenase (HADH II/ABAD) is an oxidoreductase whose salient features, include broad substrate specificity, encompassing 3-hydroxyacyl-CoA, derivatives, hydroxysteroids, alcohols and beta-hydroxybutyrate, and the, capacity to bind amyloid-beta peptide, leading to propagation of, amyloid-induced cell stress. In this study, we examine the structure and, enzymatic activity of the homologous rat HADH II/ABAD enzyme. We report, the crystal structure of rat HADH II/ABAD as a binary complex with its, NADH cofactor to 2.0 A resolution, as a ternary complex with NAD(+) and, 3-ketobutyrate (acetoacetate) to 1.4 A resolution, and as a ternary, complex with NADH and 17 beta-estradiol to 1.7 A resolution. This first, crystal ... [(full description)]
About this Structure
1E6W is a [Single protein] structure of sequence from [Rattus norvegicus] with NAD and EST as [ligands]. Active as [3-hydroxyacyl-CoA dehydrogenase], with EC number [1.1.1.35]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5, ASA, ASB, ASC and ASD. Full crystallographic information is available from [OCA].
Reference
Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD)., Powell AJ, Read JA, Banfield MJ, Gunn-Moore F, Yan SD, Lustbader J, Stern AR, Stern DM, Brady RL, J Mol Biol. 2000 Oct 20;303(2):311-27. PMID:11023795
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