1og5
STRUCTURE OF HUMAN CYTOCHROME P450 CYP2C9
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OverviewOverview
Cytochrome P450 proteins (CYP450s) are membrane-associated haem proteins, that metabolize physiologically important compounds in many species of, microorganisms, plants and animals. Mammalian CYP450s recognize and, metabolize diverse xenobiotics such as drug molecules, environmental, compounds and pollutants. Human CYP450 proteins CYP1A2, CYP2C9, CYP2C19, CYP2D6 and CYP3A4 are the major drug-metabolizing isoforms, and contribute, to the oxidative metabolism of more than 90% of the drugs in current, clinical use. Polymorphic variants have also been reported for some CYP450, isoforms, which has implications for the efficacy of drugs in individuals, and for the co-administration of drugs. The molecular basis of drug, recognition by human CYP450s, however, has remained elusive. Here we, ... [(full description)]
About this StructureAbout this Structure
1OG5 is a [Single protein] structure of sequence from [Homo sapiens] with HEC and SWF as [ligands]. Active as [Unspecific monooxygenase], with EC number [1.14.14.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of human cytochrome P450 2C9 with bound warfarin., Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H, Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. PMID:12861225
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