5fwg
From Proteopedia
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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 [[1]], with EC number [2.5.1.18]. 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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