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http://purl.uniprot.org/citations/17909281http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17909281http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17909281http://www.w3.org/2000/01/rdf-schema#comment"Mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) is a bifunctional enzyme that catalyses the oxidoreduction of the 3- and 17-hydroxy/keto groups of steroid substrates such as oestrogens, androgens and neurosteroids. The structure of the AKR1C21-NADPH binary complex was determined from an orthorhombic crystal belonging to space group P2(1)2(1)2(1) at a resolution of 1.8 A. In order to identify the factors responsible for the bifunctionality of AKR1C21, three steroid substrates including a 17-keto steroid, a 3-keto steroid and a 3alpha-hydroxysteroid were docked into the substrate-binding cavity. Models of the enzyme-coenzyme-substrate complexes suggest that Lys31, Gly225 and Gly226 are important for ligand recognition and orientation in the active site."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.org/dc/terms/identifier"doi:10.1107/s1744309107040985"xsd:string
http://purl.uniprot.org/citations/17909281http://purl.org/dc/terms/identifier"doi:10.1107/s1744309107040985"xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Endo S."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Endo S."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Hara A."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Hara A."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Carbone V."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Carbone V."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Schulze-Briese C."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Schulze-Briese C."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Chung R.P.-T."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Chung R.P.-T."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Dhagat U."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"Dhagat U."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"El-Kabbani O."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/author"El-Kabbani O."xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/name"Acta Crystallogr. F"xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/name"Acta Crystallogr. F"xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/pages"825-830"xsd:string
http://purl.uniprot.org/citations/17909281http://purl.uniprot.org/core/pages"825-830"xsd:string