1p0w - Revision history

OCA at 09:35, 16 August 2023

OCA — Wed, 16 Aug 2023 09:35:09 GMT

←Older revision		Revision as of 09:35, 16 August 2023
Line 3:		Line 3:
	<StructureSection load='1p0w' size='340' side='right'caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1p0w' size='340' side='right'caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_14581 Atcc 14581~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0W FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[1jme\|1jme]]~~, [[~~1p0v~~\|~~1p0v]], [[1p0x\|1p0x~~]]~~</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CYP102A21 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1404 ATCC 14581])</td~~><~~/tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1]~~ </~~span~~></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [https://pdbe.org/1p0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [https://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [https://pdbe.org/1p0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [https://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://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.	+	[https://www.uniprot.org/uniprot/CPXB_PRIM2 CPXB_PRIM2] Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).<ref>PMID:11695892</ref> <ref>PMID:14653735</ref> <ref>PMID:16403573</ref> <ref>PMID:16566047</ref> <ref>PMID:17077084</ref> <ref>PMID:1727637</ref> <ref>PMID:17868686</ref> <ref>PMID:18004886</ref> <ref>PMID:18020460</ref> <ref>PMID:18298086</ref> <ref>PMID:18619466</ref> <ref>PMID:18721129</ref> <ref>PMID:19492389</ref> <ref>PMID:20180779</ref> <ref>PMID:21110374</ref> <ref>PMID:21875028</ref> <ref>PMID:3106359</ref> <ref>PMID:7578081</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 14581]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Unspecific monooxygenase~~]]	+	[[Category: Priestia megaterium]]
-	[[Category: Chapman~~, S K~~]]	+	[[Category: Chapman SK]]
-	[[Category: Clark, J]]	+	[[Category: Clark J]]
-	[[Category: Daff, S]]	+	[[Category: Daff S]]
-	[[Category: Miles~~, C S~~]]	+	[[Category: Miles CS]]
-	[[Category: Mowat~~, C G~~]]	+	[[Category: Mowat CG]]
-	[[Category: Ost~~, T W.B~~]]	+	[[Category: Ost TWB]]
-	[[Category: Reid~~, G A~~]]	+	[[Category: Reid GA]]
-	[[Category: Walkinshaw~~, M D]]~~	+	[[Category: Walkinshaw MD]]
-	~~[[Category: Cytochrome p450]]~~	+
-	~~[[Category: Fatty acid hydroxylase]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 15:10, 27 October 2021

OCA — Wed, 27 Oct 2021 15:10:29 GMT

OCA at 07:20, 9 December 2020

OCA — Wed, 09 Dec 2020 07:20:28 GMT

←Older revision		Revision as of 07:20, 9 December 2020
Line 1:		Line 1:

	==F393W mutant heme domain of flavocytochrome P450 BM3==		==F393W mutant heme domain of flavocytochrome P450 BM3==
-	<StructureSection load='1p0w' size='340' side='right' caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1p0w' size='340' side='right'caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1P0W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P0W FirstGlance]. <br>
-	</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>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
	<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>		<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>
-	<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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://pdbe.org/1p0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://pdbe.org/1p0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1p0w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1p0w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 14581]]		[[Category: Atcc 14581]]
		+	[[Category: Large Structures]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
	[[Category: Chapman, S K]]		[[Category: Chapman, S K]]

OCA at 08:02, 15 February 2018

OCA — Thu, 15 Feb 2018 08:02:58 GMT

←Older revision		Revision as of 08:02, 15 February 2018
Line 1:		Line 1:
		+
	==F393W mutant heme domain of flavocytochrome P450 BM3==		==F393W mutant heme domain of flavocytochrome P450 BM3==
	<StructureSection load='1p0w' size='340' side='right' caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1p0w' size='340' side='right' caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
	<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>		<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>
-	<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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://pdbe.org/1p0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w 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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://pdbe.org/1p0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p0w_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p0w_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1p0w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1p0w" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cytochrome P450\|Cytochrome P450]]
-	*[[Flavocytochrome\|Flavocytochrome]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 05:38, 10 February 2016

OCA — Wed, 10 Feb 2016 05:38:11 GMT

←Older revision		Revision as of 05:38, 10 February 2016
Line 19:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p0w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 05:53, 11 September 2015

OCA — Fri, 11 Sep 2015 05:53:45 GMT

←Older revision		Revision as of 05:53, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1p0w' size='340' side='right' caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1p0w' size='340' side='right' caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p0w]] 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=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P0W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P0W FirstGlance]. <br>
	</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>		</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>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ~~Bacillus megaterium~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
	<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>		<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>
-	<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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w 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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://pdbe.org/1p0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1p0w" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus megaterium~~]]	+	[[Category: Atcc 14581]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
	[[Category: Chapman, S K]]		[[Category: Chapman, S K]]

OCA at 12:11, 25 December 2014

OCA — Thu, 25 Dec 2014 12:11:20 GMT

←Older revision		Revision as of 12:11, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1p0w]] 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=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P0W FirstGlance]. <br>		<table><tr><td colspan='2'>[[1p0w]] 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=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P0W FirstGlance]. <br>
-	</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>	+	</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>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>
-	<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>	+	<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>
-	<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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w 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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w 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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 39:
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]
-	[[Category: Chapman, S K.]]	+	[[Category: Chapman, S K]]
-	[[Category: Clark, J.]]	+	[[Category: Clark, J]]
-	[[Category: Daff, S.]]	+	[[Category: Daff, S]]
-	[[Category: Miles, C S.]]	+	[[Category: Miles, C S]]
-	[[Category: Mowat, C G.]]	+	[[Category: Mowat, C G]]
-	[[Category: Ost, T W.B.]]	+	[[Category: Ost, T W.B]]
-	[[Category: Reid, G A.]]	+	[[Category: Reid, G A]]
-	[[Category: Walkinshaw, M D.]]	+	[[Category: Walkinshaw, M D]]
	[[Category: Cytochrome p450]]		[[Category: Cytochrome p450]]
	[[Category: Fatty acid hydroxylase]]		[[Category: Fatty acid hydroxylase]]
	[[Category: Monooxygenase]]		[[Category: Monooxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 20:42, 28 September 2014

OCA — Sun, 28 Sep 2014 20:42:35 GMT

←Older revision		Revision as of 20:42, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1p0w.~~png~~\|~~left~~\|200px]]	+	==F393W mutant heme domain of flavocytochrome P450 BM3==
		+	<StructureSection load='1p0w' size='340' side='right' caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1p0w]] 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=1P0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P0W FirstGlance]. <br>
		+	</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>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])</td></tr>
		+	<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>
		+	<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=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [http://www.ebi.ac.uk/pdbsum/1p0w PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p0/1p0w_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In flavocytochrome P450 BM3, there is a conserved phenylalanine residue at position 393 (Phe393), close to Cys400, the thiolate ligand to the heme. Substitution of Phe393 by Ala, His, Tyr, and Trp has allowed us to modulate the reduction potential of the heme, while retaining the structural integrity of the enzyme's active site. Substrate binding triggers electron transfer in P450 BM3 by inducing a shift from a low- to high-spin ferric heme and a 140 mV increase in the heme reduction potential. Kinetic analysis of the mutants indicated that the spin-state shift alone accelerates the rate of heme reduction (the rate determining step for overall catalysis) by 200-fold and that the concomitant shift in reduction potential is only responsible for a modest 2-fold rate enhancement. The second step in the P450 catalytic cycle involves binding of dioxygen to the ferrous heme. The stabilities of the oxy-ferrous complexes in the mutant enzymes were also analyzed using stopped-flow kinetics. These were found to be surprisingly stable, decaying to superoxide and ferric heme at rates of 0.01-0.5 s(-)(1). The stability of the oxy-ferrous complexes was greater for mutants with higher reduction potentials, which had lower catalytic turnover rates but faster heme reduction rates. The catalytic rate-determining step of these enzymes can no longer be the initial heme reduction event but is likely to be either reduction of the stabilized oxy-ferrous complex, i.e., the second flavin to heme electron transfer or a subsequent protonation event. Modulating the reduction potential of P450 BM3 appears to tune the two steps in opposite directions; the potential of the wild-type enzyme appears to be optimized to maximize the overall rate of turnover. The dependence of the visible absorption spectrum of the oxy-ferrous complex on the heme reduction potential is also discussed.

-	~~{{STRUCTURE_1p0w\| PDB=1p0w \| SCENE= }}~~	+	Oxygen activation and electron transfer in flavocytochrome P450 BM3.,Ost TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S J Am Chem Soc. 2003 Dec 10;125(49):15010-20. PMID:14653735<ref>PMID:14653735</ref>

-	~~===F393W mutant heme domain~~ of ~~flavocytochrome P450 BM3===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_14653735}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1p0w]] 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=1P0W OCA].~~	+

	==See Also==		==See Also==
		+	*[[Cytochrome P450\|Cytochrome P450]]
	*[[Flavocytochrome\|Flavocytochrome]]		*[[Flavocytochrome\|Flavocytochrome]]
-	*[[NADPH-Cytochrome P450 Reductase\|NADPH-Cytochrome P450 Reductase]]	+	== References ==
-		+	<references/>
-	==~~Reference~~==	+	__TOC__
-	<~~ref group="xtra">PMID:014653735<~~/~~ref~~><~~ref group="xtra">PMID:012651851</ref><references group="xtra"~~/>	+	</StructureSection>
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]

OCA at 16:30, 20 October 2012

OCA — Sat, 20 Oct 2012 16:30:39 GMT

←Older revision		Revision as of 16:30, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1p0w]] is a 2 chain structure ~~of [[Flavocytochrome]] and [[NADPH-Cytochrome P450 Reductase]]~~ 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=1P0W OCA].	+	[[1p0w]] 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=1P0W OCA].

	==See Also==		==See Also==

OCA at 21:55, 26 July 2012

OCA — Thu, 26 Jul 2012 21:55:29 GMT

←Older revision		Revision as of 21:55, 26 July 2012
Line 1:		Line 1:
	[[Image:1p0w.png\|left\|200px]]		[[Image:1p0w.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1p0w", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1p0w\| PDB=1p0w \| SCENE= }}		{{STRUCTURE_1p0w\| PDB=1p0w \| SCENE= }}

	===F393W mutant heme domain of flavocytochrome P450 BM3===		===F393W mutant heme domain of flavocytochrome P450 BM3===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_14653735}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 14653735 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_14653735}}		{{ABSTRACT_PUBMED_14653735}}

	==About this Structure==		==About this Structure==
-	[[1p0w]] is a 2 chain structure of [[Cytochrome P450]] 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=1P0W OCA].	+	[[1p0w]] is a 2 chain structure of [[Flavocytochrome]] and [[NADPH-Cytochrome P450 Reductase]] 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=1P0W OCA].

	==See Also==		==See Also==
-	*[[Cytochrome P450]]	+	*[[Flavocytochrome\|Flavocytochrome]]
		+	*[[NADPH-Cytochrome P450 Reductase\|NADPH-Cytochrome P450 Reductase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~14653735~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:014653735</ref><ref group="xtra">PMID:012651851</ref><references group="xtra"/>
	[[Category: Bacillus megaterium]]		[[Category: Bacillus megaterium]]
	[[Category: Unspecific monooxygenase]]		[[Category: Unspecific monooxygenase]]

←Older revision		Revision as of 15:10, 27 October 2021
Line 3:		Line 3:
	<StructureSection load='1p0w' size='340' side='right'caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1p0w' size='340' side='right'caption='[[1p0w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1P0W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1p0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jme\|1jme]], [[1p0v\|1p0v]], [[1p0x\|1p0x]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CYP102A21 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr>
-	<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>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [~~http~~://pdbe.org/1p0w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0w OCA], [https://pdbe.org/1p0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0w RCSB], [https://www.ebi.ac.uk/pdbsum/1p0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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.	+	[[https://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]]