RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/8331657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8331657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8331657http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these domains via a network of hydrogen bonds and salt-links. In particular, the sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is completely buried in a hydrophobic pocket. The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain". The main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1993.1376"xsd:string
http://purl.uniprot.org/citations/8331657http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1993.1376"xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Huber R."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Huber R."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Kleywegt G.J."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Kleywegt G.J."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Jones T.A."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Jones T.A."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Gilliland G.L."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Gilliland G.L."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Ji X."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Ji X."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Board P.G."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Board P.G."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Reinemer P."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Reinemer P."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Sinning I."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Sinning I."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Cowan S.W."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Cowan S.W."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Armstrong R.N."xsd:string
http://purl.uniprot.org/citations/8331657http://purl.uniprot.org/core/author"Armstrong R.N."xsd:string