5xhj - Revision history

OCA at 08:02, 22 November 2023

OCA — Wed, 22 Nov 2023 08:02:16 GMT

←Older revision		Revision as of 08:02, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='5xhj' size='340' side='right'caption='[[5xhj]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5xhj' size='340' side='right'caption='[[5xhj]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xhj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5XHJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xhj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_NBRC_15308_=_ATCC_14581 Priestia megaterium NBRC 15308 = ATCC 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XHJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=87X:5-cyclohexylpentanoic+acid'>87X</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5xhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhj OCA], [~~http~~://pdbe.org/5xhj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xhj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xhj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhj ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=87X:5-cyclohexylpentanoic+acid'>87X</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></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=5xhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhj OCA], [https://pdbe.org/5xhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xhj RCSB], [https://www.ebi.ac.uk/pdbsum/5xhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhj 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 18:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kasai, C]]	+	[[Category: Priestia megaterium NBRC 15308 = ATCC 14581]]
-	[[Category: Shiro, Y]]	+	[[Category: Kasai C]]
-	[[Category: Shoji, O]]	+	[[Category: Shiro Y]]
-	[[Category: Stanfield~~, J K~~]]	+	[[Category: Shoji O]]
-	[[Category: Sugimoto, H]]	+	[[Category: Stanfield JK]]
-	[[Category: Suzuki, K]]	+	[[Category: Sugimoto H]]
-	[[Category: Watanabe, Y]]	+	[[Category: Suzuki K]]
-	~~[[Category: Cytochrome p450]]~~	+	[[Category: Watanabe Y]]
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 06:49, 14 October 2020

OCA — Wed, 14 Oct 2020 06:49:48 GMT

←Older revision		Revision as of 06:49, 14 October 2020
Line 1:		Line 1:

	==Crystal Structure of P450BM3 with 5-Cyclohexylvaleroyl-L-Tryptophan==		==Crystal Structure of P450BM3 with 5-Cyclohexylvaleroyl-L-Tryptophan==
-	<StructureSection load='5xhj' size='340' side='right' caption='[[5xhj]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5xhj' size='340' side='right'caption='[[5xhj]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xhj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHJ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XHJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xhj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XHJ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=87X:5-cyclohexylpentanoic+acid'>87X</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=87X:5-cyclohexylpentanoic+acid'>87X</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></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=5xhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhj OCA], [http://pdbe.org/5xhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xhj RCSB], [http://www.ebi.ac.uk/pdbsum/5xhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhj 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=5xhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhj OCA], [http://pdbe.org/5xhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xhj RCSB], [http://www.ebi.ac.uk/pdbsum/5xhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhj 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>		[[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 ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Kasai, C]]		[[Category: Kasai, C]]
	[[Category: Shiro, Y]]		[[Category: Shiro, Y]]

OCA at 07:19, 6 December 2017

OCA — Wed, 06 Dec 2017 07:19:50 GMT

←Older revision		Revision as of 07:19, 6 December 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5xhj is ~~ON HOLD~~	+	==Crystal Structure of P450BM3 with 5-Cyclohexylvaleroyl-L-Tryptophan==
-		+	<StructureSection load='5xhj' size='340' side='right' caption='[[5xhj]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~Authors~~: ~~Suzuki~~, K., ~~Shoji~~, O., ~~Stanfield~~, J.K., ~~Kasai~~, C., ~~Sugimoto~~, H., ~~Shiro~~, Y., ~~Watanabe~~, Y.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5xhj]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XHJ FirstGlance]. <br>
-	~~Description~~: ~~Crystal Structure~~ of ~~P450BM3 with 5~~-~~Cyclohexylvaleroyl~~-L-~~Tryptophan~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=87X:5-cyclohexylpentanoic+acid'>87X</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=5xhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xhj OCA], [http://pdbe.org/5xhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xhj RCSB], [http://www.ebi.ac.uk/pdbsum/5xhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xhj ProSAT]</span></td></tr>
		+	</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>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Kasai, C]]
	[[Category: Shiro, Y]]		[[Category: Shiro, Y]]
		+	[[Category: Shoji, O]]
		+	[[Category: Stanfield, J K]]
	[[Category: Sugimoto, H]]		[[Category: Sugimoto, H]]
-	[[Category: Shoji, O]]
	[[Category: Suzuki, K]]		[[Category: Suzuki, K]]
-	[[Category: Kasai, C]]
-	[[Category: Stanfield, J.K]]
	[[Category: Watanabe, Y]]		[[Category: Watanabe, Y]]
		+	[[Category: Cytochrome p450]]
		+	[[Category: Oxidoreductase]]

OCA at 15:28, 27 September 2017

OCA — Wed, 27 Sep 2017 15:28:36 GMT

←Older revision		Revision as of 15:28, 27 September 2017
Line 8:		Line 8:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Shiro, Y]]		[[Category: Shiro, Y]]
-	[[Category: Stanfield, J.K]]
	[[Category: Sugimoto, H]]		[[Category: Sugimoto, H]]
	[[Category: Shoji, O]]		[[Category: Shoji, O]]
-	[[Category: Watanabe, Y]]
	[[Category: Suzuki, K]]		[[Category: Suzuki, K]]
	[[Category: Kasai, C]]		[[Category: Kasai, C]]
		+	[[Category: Stanfield, J.K]]
		+	[[Category: Watanabe, Y]]

OCA at 12:29, 24 May 2017

OCA — Wed, 24 May 2017 12:29:07 GMT

←Older revision		Revision as of 12:29, 24 May 2017
Line 3:		Line 3:
	The entry 5xhj is ON HOLD		The entry 5xhj is ON HOLD

-	Authors: Suzuki, K., Shoji, O., Stanfield, J.K., Kasai, C, Sugimoto, H., Shiro, Y., Watanabe, Y.	+	Authors: Suzuki, K., Shoji, O., Stanfield, J.K., Kasai, C., Sugimoto, H., Shiro, Y., Watanabe, Y.

	Description: Crystal Structure of P450BM3 with 5-Cyclohexylvaleroyl-L-Tryptophan		Description: Crystal Structure of P450BM3 with 5-Cyclohexylvaleroyl-L-Tryptophan
Line 9:		Line 9:
	[[Category: Shiro, Y]]		[[Category: Shiro, Y]]
	[[Category: Stanfield, J.K]]		[[Category: Stanfield, J.K]]
-	[[Category: ~~Kasai, C,~~ Sugimoto, H]]	+	[[Category: Sugimoto, H]]
	[[Category: Shoji, O]]		[[Category: Shoji, O]]
	[[Category: Watanabe, Y]]		[[Category: Watanabe, Y]]
	[[Category: Suzuki, K]]		[[Category: Suzuki, K]]
		+	[[Category: Kasai, C]]

OCA: Protected "5xhj" [edit=sysop:move=sysop]

OCA — Thu, 27 Apr 2017 13:05:29 GMT

Protected "5xhj" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:05, 27 April 2017

OCA: New page: '''Unreleased structure''' The entry 5xhj is ON HOLD Authors: Suzuki, K., Shoji, O., Stanfield, J.K., Kasai, C, Sugimoto, H., Shiro, Y., Watanabe, Y. Description: Crystal Structure of ...

OCA — Thu, 27 Apr 2017 13:05:28 GMT

New page: '''Unreleased structure''' The entry 5xhj is ON HOLD Authors: Suzuki, K., Shoji, O., Stanfield, J.K., Kasai, C, Sugimoto, H., Shiro, Y., Watanabe, Y. Description: Crystal Structure of ...

New page

'''Unreleased structure'''

The entry 5xhj is ON HOLD

Authors: Suzuki, K., Shoji, O., Stanfield, J.K., Kasai, C, Sugimoto, H., Shiro, Y., Watanabe, Y.

Description: Crystal Structure of P450BM3 with 5-Cyclohexylvaleroyl-L-Tryptophan
[[Category: Unreleased Structures]]
[[Category: Shiro, Y]]
[[Category: Stanfield, J.K]]
[[Category: Kasai, C, Sugimoto, H]]
[[Category: Shoji, O]]
[[Category: Watanabe, Y]]
[[Category: Suzuki, K]]