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3hf2

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HF2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HF2 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P450BM-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P450BM-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hf2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hf2 RCSB], [http://www.ebi.ac.uk/pdbsum/3hf2 PDBsum]</span></td></tr>
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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=3hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hf2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hf2 RCSB], [http://www.ebi.ac.uk/pdbsum/3hf2 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Bacillus megaterium]]
[[Category: Bacillus megaterium]]
[[Category: Unspecific monooxygenase]]
[[Category: Unspecific monooxygenase]]
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[[Category: Bartlam, M.]]
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[[Category: Bartlam, M]]
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[[Category: Bell, S G.]]
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[[Category: Bell, S G]]
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[[Category: Rao, Z.]]
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[[Category: Rao, Z]]
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[[Category: Whitehouse, C J.C.]]
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[[Category: Whitehouse, C J.C]]
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[[Category: Wong, L L.]]
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[[Category: Wong, L L]]
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[[Category: Yang, W.]]
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[[Category: Yang, W]]
[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Fad]]
[[Category: Fad]]

Revision as of 18:54, 25 December 2014

Crystal structure of the I401P mutant of cytochrome P450 BM3

3hf2, resolution 2.20Å

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