4jlt
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jlt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jlt RCSB], [http://www.ebi.ac.uk/pdbsum/4jlt PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jlt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jlt RCSB], [http://www.ebi.ac.uk/pdbsum/4jlt PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CP2B4_RABIT CP2B4_RABIT]] 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. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 17:49, 25 December 2014
Crystal structure of P450 2B4(H226Y) in complex with paroxetine
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