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http://purl.uniprot.org/SHA-384/CEA16C580678CC473DB994E9C9203B93E5FA3BFA27331DC68EBA67E4B1C656EAB30E76440FF3296C35010E5995F9910Dhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/CEA16C580678CC473DB994E9C9203B93E5FA3BFA27331DC68EBA67E4B1C656EAB30E76440FF3296C35010E5995F9910Dhttp://www.w3.org/2000/01/rdf-schema#comment"Data suggest that binding sites between CYP11B1/CYP11B2 and adrenodoxin/ferredoxin-1 exhibit electrostatic interactions at K370 in CYP11B1 and at K366 in CYP11B2 mutant R366K with D79 in adrenodoxin/ferredoxin-1. (CYP11B1 = cytochrome P450 family 11 subfamily B member 1; CYP11B2 = cytochrome P450 family 11 subfamily B member 2)"xsd:string
http://purl.uniprot.org/uniprot/#_7406AB488B7C2148CF4321EAF13F8BAE65D1355852E027C271C4757785C568261E9C171707956F1312AC0D9D2E21DDCBhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/CEA16C580678CC473DB994E9C9203B93E5FA3BFA27331DC68EBA67E4B1C656EAB30E76440FF3296C35010E5995F9910D
http://purl.uniprot.org/uniprot/P10109http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/CEA16C580678CC473DB994E9C9203B93E5FA3BFA27331DC68EBA67E4B1C656EAB30E76440FF3296C35010E5995F9910D
http://purl.uniprot.org/uniprot/#_P10109-mappedCitation-28355486http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/CEA16C580678CC473DB994E9C9203B93E5FA3BFA27331DC68EBA67E4B1C656EAB30E76440FF3296C35010E5995F9910D