1rrh
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1RRH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Glycine_max Glycine max]] with FE2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1RRH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Glycine_max Glycine max]] with FE2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RRH OCA]]. |
==Reference== | ==Reference== | ||
Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution., Skrzypczak-Jankun E, Borbulevych OY, Zavodszky MI, Baranski MR, Padmanabhan K, Petricek V, Jankun J, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):766-75. Epub 2006, Jun 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16790932 16790932] | Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution., Skrzypczak-Jankun E, Borbulevych OY, Zavodszky MI, Baranski MR, Padmanabhan K, Petricek V, Jankun J, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):766-75. Epub 2006, Jun 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16790932 16790932] | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
| + | [[Category: Lipoxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Borbulevych, O.Y.]] | [[Category: Borbulevych, O.Y.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:02:42 2007'' |
Revision as of 07:58, 30 October 2007
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Soybean Lipoxygenase (LOX-3) at ambient temperatures at 2.0 A resolution
Overview
Flash-freezing is a technique that is commonly used nowadays to collect, diffraction data for X-ray structural analysis. It can affect both the, crystal and molecular structure and the molecule's surface, as well as the, internal cavities. X-ray structural data often serve as a template for the, protein receptor in docking calculations. Thus, the size and shape of the, binding site determines which small molecules could be found as potential, ligands in silico, especially during high-throughput rigid docking. Data, were analyzed for wild soybean lipoxygenase-3 (MW 97 kDa) at 293 and 93 K, and compared with the results from studies of its molecular complexes with, known inhibitors, structures published by others for a derivative of the, same enzyme (98 K) or a topologically close isozyme ... [(full description)]
About this Structure
1RRH is a [Single protein] structure of sequence from [Glycine max] with FE2 as [ligand]. Active as [Lipoxygenase], with EC number [1.13.11.12]. Full crystallographic information is available from [OCA].
Reference
Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution., Skrzypczak-Jankun E, Borbulevych OY, Zavodszky MI, Baranski MR, Padmanabhan K, Petricek V, Jankun J, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):766-75. Epub 2006, Jun 20. PMID:16790932
Page seeded by OCA on Tue Oct 30 10:02:42 2007
