6k3q - Revision history

OCA at 10:26, 22 November 2023

2023-11-22T10:26:21Z

←Older revision		Revision as of 10:26, 22 November 2023
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	<StructureSection load='6k3q' size='340' side='right'caption='[[6k3q]], [[Resolution\|resolution]] 2.06Å' scene=''>		<StructureSection load='6k3q' size='340' side='right'caption='[[6k3q]], [[Resolution\|resolution]] 2.06Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6k3q]] 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=6K3Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6K3Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6k3q]] 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=6K3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K3Q FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D0F:(2S)-2-[[(2S)-1-(3-cyclohexylpropanoyl)pyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic+acid'>D0F</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <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]] 2.06Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">cyp102A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D0F:(2S)-2-[[(2S)-1-(3-cyclohexylpropanoyl)pyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic+acid'>D0F</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=6k3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3q OCA], [~~http~~://pdbe.org/6k3q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6k3q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6k3q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3q 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=6k3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3q OCA], [https://pdbe.org/6k3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k3q RCSB], [https://www.ebi.ac.uk/pdbsum/6k3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~CPXB_BACMB CPXB_BACMB]~~] 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>	+	[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>

	==See Also==		==See Also==
Line 17:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 14581]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Shoji, O~~]]	+	[[Category: Priestia megaterium]]
-	[[Category: ~~Yonemura, K~~]]	+	[[Category: Shoji O]]
-	[[Category: ~~Monooxygenase]]~~	+	[[Category: Yonemura K]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:59, 6 January 2021

2021-01-06T08:59:33Z

←Older revision		Revision as of 08:59, 6 January 2021
Line 1:		Line 1:

	==Crystal Structure of P450BM3 with N-(3-cyclohexylpropanoyl)-L-prolyl-L-phenylalanine==		==Crystal Structure of P450BM3 with N-(3-cyclohexylpropanoyl)-L-prolyl-L-phenylalanine==
-	<StructureSection load='6k3q' size='340' side='right'caption='[[6k3q]]' scene=''>	+	<StructureSection load='6k3q' size='340' side='right'caption='[[6k3q]], [[Resolution\|resolution]] 2.06Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K3Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K3Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6k3q]] 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=6K3Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K3Q FirstGlance]. <br>
-	</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=6k3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3q OCA], [http://pdbe.org/6k3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k3q RCSB], [http://www.ebi.ac.uk/pdbsum/6k3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3q ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D0F:(2S)-2-[[(2S)-1-(3-cyclohexylpropanoyl)pyrrolidin-2-yl]carbonylamino]-3-phenyl-propanoic+acid'>D0F</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <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">cyp102A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</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=6k3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3q OCA], [http://pdbe.org/6k3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k3q RCSB], [http://www.ebi.ac.uk/pdbsum/6k3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3q ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CPXB_BACMB CPXB_BACMB]] 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>
		+
		+	==See Also==
		+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 14581]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Shoji O]]	+	[[Category: Shoji, O]]
-	[[Category: Yonemura K]]	+	[[Category: Yonemura, K]]
		+	[[Category: Monooxygenase]]
		+	[[Category: Oxidoreductase]]

OCA at 06:51, 27 May 2020

2020-05-27T06:51:44Z

←Older revision		Revision as of 06:51, 27 May 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6k3q ~~is ON HOLD until May 21 2021~~	+	==Crystal Structure of P450BM3 with N-(3-cyclohexylpropanoyl)-L-prolyl-L-phenylalanine==
-		+	<StructureSection load='6k3q' size='340' side='right'caption='[[6k3q]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K3Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K3Q FirstGlance]. <br>
-	~~Description~~:	+	</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=6k3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k3q OCA], [http://pdbe.org/6k3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k3q RCSB], [http://www.ebi.ac.uk/pdbsum/6k3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k3q ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Shoji O]]
		+	[[Category: Yonemura K]]

OCA at 04:02, 19 June 2019

2019-06-19T04:02:57Z

←Older revision		Revision as of 04:02, 19 June 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6k3q is ON HOLD	+	The entry 6k3q is ON HOLD until May 21 2021

	Authors:		Authors:

OCA: Protected "6k3q" [edit=sysop:move=sysop]

2019-05-29T04:25:55Z

Protected "6k3q" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:25, 29 May 2019

OCA: New page: '''Unreleased structure''' The entry 6k3q is ON HOLD Authors: Description: Category: Unreleased Structures

2019-05-29T04:25:54Z

New page: '''Unreleased structure''' The entry 6k3q is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6k3q is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]