4hgh
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=4hgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hgh RCSB], [http://www.ebi.ac.uk/pdbsum/4hgh 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=4hgh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hgh RCSB], [http://www.ebi.ac.uk/pdbsum/4hgh PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 22:39, 24 December 2014
Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset I)
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