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5fwg
From Proteopedia
(New page: 200px<br /> <applet load="5fwg" size="450" color="white" frame="true" align="right" spinBox="true" caption="5fwg, resolution 2.0Å" /> '''TETRA-(5-FLUOROTRYPT...) |
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==About this Structure== | ==About this Structure== | ||
| - | 5FWG 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 GPR 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=2.5.1.18 2.5.1.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]]. | + | 5FWG 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 GPR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18]]. Structure known Active Site: GPS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5FWG OCA]]. |
==Reference== | ==Reference== | ||
Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene., Ji X, Johnson WW, Sesay MA, Dickert L, Prasad SM, Ammon HL, Armstrong RN, Gilliland GL, Biochemistry. 1994 Feb 8;33(5):1043-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8110735 8110735] | Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene., Ji X, Johnson WW, Sesay MA, Dickert L, Prasad SM, Ammon HL, Armstrong RN, Gilliland GL, Biochemistry. 1994 Feb 8;33(5):1043-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8110735 8110735] | ||
| + | [[Category: Glutathione transferase]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: unnatural amino acid]] | [[Category: unnatural amino acid]] | ||
| - | ''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 13:29:19 2007'' |
Revision as of 11:24, 30 October 2007
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TETRA-(5-FLUOROTRYPTOPHANYL)-GLUTATHIONE TRANSFERASE
Overview
The three-dimensional structures of isoenzyme 3-3 of glutathione (GSH), transferase complexed with (9R,10R)- and, (9S,10S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene, [(9R,10R)-2 and (9S,10S)-2], which are the products of the addition of GSH, to phenanthrene 9,10-oxide, have been determined at resolutions of 1.9 and, 1.8 A, respectively. The structures indicate that the xenobiotic substrate, binding site is a hydrophobic cavity defined by the side chains of Y6, W7, V9, and L12 from domain I (the GSH binding domain) and I111, Y115, F208, and S209 in domain II of the protein. All of these residues are located in, variable-sequence regions of the primary structure of class mu isoenzymes., Three of the eight residues (V9, I111, and S209) of isoenzyme 3-3 that are, in direct van ... [(full description)]
About this Structure
5FWG is a [Single protein] structure of sequence from [Rattus norvegicus] with GPR as [ligand]. Active as [Glutathione transferase], with EC number [2.5.1.18]. Structure known Active Site: GPS. Full crystallographic information is available from [OCA].
Reference
Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene., Ji X, Johnson WW, Sesay MA, Dickert L, Prasad SM, Ammon HL, Armstrong RN, Gilliland GL, Biochemistry. 1994 Feb 8;33(5):1043-52. PMID:8110735
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