4i91

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'''Unreleased structure'''
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{{STRUCTURE_4i91| PDB=4i91 | SCENE= }}
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===Crystal Structure of Cytochrome P450 2B6 (Y226H/K262R) in complex with alpha-Pinene.===
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The entry 4i91 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/CP2B6_HUMAN 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.<ref>PMID:11695850</ref>
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Authors: Shah, M.B., Stout, C.D., Halpert, J.R.
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==About this Structure==
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[[4i91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I91 OCA].
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Description: Crystal Structure of Cytochrome P450 2B6 (Y226H/K262R) in complex with alpha-Pinene.
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Halpert, J R.]]
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[[Category: Shah, M B.]]
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[[Category: Stout, C D.]]
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[[Category: Cyp2b6]]
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[[Category: Cytochrome p450 2b6]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Heme]]
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[[Category: Iron]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Metal binding]]
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[[Category: Microsome]]
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[[Category: Monooxygenase]]
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[[Category: Oxidoreductase]]
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[[Category: P450]]

Revision as of 14:16, 3 July 2013

Template:STRUCTURE 4i91

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

  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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