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http://purl.uniprot.org/citations/9245401http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9245401http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9245401http://www.w3.org/2000/01/rdf-schema#comment"Complex structures of a naturally occurring variant of human class pi glutathione S-transferase 1-1 (hGSTP1-1) with either S-hexylglutathione or (9R,10R)-9-(S-glutathionyl)-10-hydroxy-9, 10-dihydrophenanthrene [(9R,10R)-GSPhen] have been determined at resolutions of 1.8 and 1.9 A, respectively. The crystal structures reveal that the xenobiotic substrate-binding site (H-site) is located at a position similar to that observed in class mu GST 1-1 from rat liver (rGSTM1-1). In rGSTM1-1, the H-site is a hydrophobic cavity defined by the side chains of Y6, W7, V9, L12, I111, Y115, F208, and S209. In hGSTP1-1, the cavity is approximately half hydrophobic and half hydrophilic and is defined by the side chains of Y7, F8, V10, R13, V104, Y108, N204, and G205 and five water molecules. A hydrogen bond network connects the five water molecules and the side chains of R13 and N204. V104 is positioned such that the introduction of a methyl group (the result of the V104I mutation) disturbs the H-site water structure and alters the substrate-binding properties of the isozyme. The hydroxyl group of Y7 forms a hydrogen bond (3.2 A) with the sulfur atom of the product. There is a short hydrogen bond (2.5 A) between Y108 (OH) and (9R, 10R)-GSPhen (O5), indicating the hydroxyl group of Y108 as an electrophilic participant in the addition of glutathione to epoxides. An N-(2-hydroxethyl)piperazine-N'-2-ethanesulfonic acid (HEPES) molecule is found in the cavity between beta2 and alphaI. The location and properties of this HEPES-binding site fit a possible non-substrate-binding site that is involved in noncompetitive inhibition of the enzyme."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.org/dc/terms/identifier"doi:10.1021/bi970805s"xsd:string
http://purl.uniprot.org/citations/9245401http://purl.org/dc/terms/identifier"doi:10.1021/bi970805s"xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Gilliland G.L."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Gilliland G.L."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Ji X."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Ji X."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Tordova M."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Tordova M."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Parsons J.F."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Parsons J.F."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Zimniak P."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Zimniak P."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Hayden J.B."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"Hayden J.B."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"O'Donnell R."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/author"O'Donnell R."xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/pages"9690-9702"xsd:string
http://purl.uniprot.org/citations/9245401http://purl.uniprot.org/core/pages"9690-9702"xsd:string