4i91

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Template:STRUCTURE 4i91

Contents

Crystal Structure of Cytochrome P450 2B6 (Y226H/K262R) in complex with alpha-Pinene.

Template:ABSTRACT PUBMED 23786449

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.

See Also

Reference

  • Wilderman PR, Shah MB, Jang HH, Stout CD, Halpert JR. Structural and Thermodynamic Basis of (+)-alpha-Pinene Binding to Human Cytochrome P450 2B6. J Am Chem Soc. 2013 Jul 17;135(28):10433-40. doi: 10.1021/ja403042k. Epub 2013, Jul 3. PMID:23786449 doi:10.1021/ja403042k
  1. ↑ 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

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