4jlt

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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>
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== Function ==
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[[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.
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== 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

4jlt, resolution 2.14Å

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