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http://purl.uniprot.org/SHA-384/769CDB6A56BE11C2EFBBDD84FBA0F3232CDA2C19AEF911A42AEC1444180DAED9FA4B8205D6D3422C3327E71C19ED9C3Ehttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/769CDB6A56BE11C2EFBBDD84FBA0F3232CDA2C19AEF911A42AEC1444180DAED9FA4B8205D6D3422C3327E71C19ED9C3Ehttp://www.w3.org/2000/01/rdf-schema#comment"A single-point mutation at asparagine 202 in the active site pocket of CYP17A1 even when far from the heme has profound effects on steroidogenic selectivity in androgen biosynthesis. In the mutant the 17alpha alcohol of OHPROG forms a H-bond with the proximal rather than terminal oxygen of the oxy-ferrous complex.When OHPREG was a substrate the mutant was found to have weak H-bonding interaction with the proximal ox..."xsd:string
http://purl.uniprot.org/uniprot/#_9A24B3F380195D8F12029A9710B720FF934E991458A7D73A034C2DBFB6FE8D9EEB4F57F5E9D4E93230E7F360DEC1FF8Fhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/769CDB6A56BE11C2EFBBDD84FBA0F3232CDA2C19AEF911A42AEC1444180DAED9FA4B8205D6D3422C3327E71C19ED9C3E
http://purl.uniprot.org/uniprot/Q1HB44http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/769CDB6A56BE11C2EFBBDD84FBA0F3232CDA2C19AEF911A42AEC1444180DAED9FA4B8205D6D3422C3327E71C19ED9C3E
http://purl.uniprot.org/uniprot/#_Q1HB44-mappedCitation-29283561http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/769CDB6A56BE11C2EFBBDD84FBA0F3232CDA2C19AEF911A42AEC1444180DAED9FA4B8205D6D3422C3327E71C19ED9C3E