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4i91
From Proteopedia
Contents |
Crystal Structure of Cytochrome P450 2B6 (Y226H/K262R) in complex with alpha-Pinene.
Function
[CP2B6_HUMAN] Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase.[1]
About this Structure
4i91 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Miyazawa M, Shindo M, Shimada T. Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-cineole, a monoterpene cyclic ether, by rat and human liver microsomes. Xenobiotica. 2001 Oct;31(10):713-23. PMID:11695850 doi:10.1080/00498250110065595
Categories: Homo sapiens | Halpert, J R. | Shah, M B. | Stout, C D. | Cyp2b6 | Cytochrome p450 2b6 | Endoplasmic reticulum | Heme | Iron | Membrane | Membrane protein | Metal binding | Microsome | Monooxygenase | Oxidoreductase | P450
