4w9n - Revision history

OCA at 07:29, 27 September 2023

OCA — Wed, 27 Sep 2023 07:29:14 GMT

←Older revision		Revision as of 07:29, 27 September 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W9N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W9N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</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]] 1.84Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [https://pdbe.org/4w9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [https://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n 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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [https://pdbe.org/4w9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [https://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:58, 7 April 2023

OCA — Fri, 07 Apr 2023 06:58:31 GMT

←Older revision		Revision as of 06:58, 7 April 2023
Line 3:		Line 3:
	<StructureSection load='4w9n' size='340' side='right'caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>		<StructureSection load='4w9n' size='340' side='right'caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4W9N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W9N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [https://pdbe.org/4w9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [https://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4w82\|4w82]]</td></tr>~~	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FASN, FAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [~~http~~://pdbe.org/4w9n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.	+	[https://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
-	*[[Enoyl-Acyl-Carrier Protein Reductase\|Enoyl-Acyl-Carrier Protein Reductase]]	+	*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures\|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Quiocho~~, F A~~]]	+	[[Category: Quiocho FA]]
-	[[Category: Sankaran, B]]	+	[[Category: Sankaran B]]
-	[[Category: Sippel~~, K H~~]]	+	[[Category: Sippel KH]]
-	[[Category: Vyas~~, N K]]~~	+	[[Category: Vyas NK]]
-	~~[[Category: Enoyl reductase]]~~	+
-	~~[[Category: Fatty acid metabolism]]~~	+
-	~~[[Category: Fatty acid synthase]]~~	+
-	~~[[Category: Nadph-dependent]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 08:23, 23 May 2019

OCA — Thu, 23 May 2019 08:23:41 GMT

←Older revision		Revision as of 08:23, 23 May 2019
Line 1:		Line 1:

	==Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan==		==Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan==
-	<StructureSection load='4w9n' size='340' side='right' caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>	+	<StructureSection load='4w9n' size='340' side='right'caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W9N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W9N FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4w82\|4w82]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4w82\|4w82]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FASN, FAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://pdbe.org/4w9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n ProSAT]</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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://pdbe.org/4w9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n ProSAT]</span></td></tr>
Line 21:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 4w9n" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4w9n" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Enoyl-Acyl-Carrier Protein Reductase\|Enoyl-Acyl-Carrier Protein Reductase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Quiocho, F A]]		[[Category: Quiocho, F A]]
	[[Category: Sankaran, B]]		[[Category: Sankaran, B]]
Line 33:		Line 39:
	[[Category: Fatty acid synthase]]		[[Category: Fatty acid synthase]]
	[[Category: Nadph-dependent]]		[[Category: Nadph-dependent]]
		+	[[Category: Oxidoreductase]]

OCA at 11:17, 4 August 2016

OCA — Thu, 04 Aug 2016 11:17:21 GMT

←Older revision		Revision as of 11:17, 4 August 2016
Line 1:		Line 1:
		+
	==Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan==		==Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan==
	<StructureSection load='4w9n' size='340' side='right' caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>		<StructureSection load='4w9n' size='340' side='right' caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4w82\|4w82]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4w82\|4w82]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n 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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://pdbe.org/4w9n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9n ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4w9n" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:46, 25 December 2014

OCA — Thu, 25 Dec 2014 08:46:03 GMT

←Older revision		Revision as of 08:46, 25 December 2014
Line 9:		Line 9:
	<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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n 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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 12:00, 10 December 2014

OCA — Wed, 10 Dec 2014 12:00:40 GMT

←Older revision		Revision as of 12:00, 10 December 2014
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Quiocho, F A.]]	+	[[Category: Quiocho, F A]]
-	[[Category: Sankaran, B.]]	+	[[Category: Sankaran, B]]
-	[[Category: Sippel, K H.]]	+	[[Category: Sippel, K H]]
-	[[Category: Vyas, N K.]]	+	[[Category: Vyas, N K]]
	[[Category: Enoyl reductase]]		[[Category: Enoyl reductase]]
	[[Category: Fatty acid metabolism]]		[[Category: Fatty acid metabolism]]
	[[Category: Fatty acid synthase]]		[[Category: Fatty acid synthase]]
	[[Category: Nadph-dependent]]		[[Category: Nadph-dependent]]

OCA at 08:31, 22 October 2014

OCA — Wed, 22 Oct 2014 08:31:52 GMT

←Older revision		Revision as of 08:31, 22 October 2014
Line 9:		Line 9:
	<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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n 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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human fatty acid synthase (FAS) is a large, multidomain protein that synthesizes long-chain fatty acids. Since these fatty acids are primarily provided by diet, FAS is normally expressed at low levels; however, it is highly upregulated in many cancers. Human enoyl-acyl carrier protein-reductase (hER) is one of the FAS catalytic domains and its inhibition by drugs like triclosan (TCL) can increase cytotoxicity and decrease drug resistance in cancer cells. We have determined the structure of hER in the presence and absence of TCL. TCL was not bound in the active site, as predicted, but rather at the protein-protein interface (PPI). TCL binding induces a dimer orientation change that causes downstream structural rearrangement in critical active site residues. Kinetics studies indicate that TCL is capable of inhibiting the isolated hER domain with an IC50 of approximately 55 muM. Given the hER-TCL structure and the inhibition observed in the hER domain, it seems likely that TCL is observed in the physiologically relevant binding site and that it acts as an allosteric PPI inhibitor. TCL may be a viable scaffold for the development of anti-cancer PPI FAS inhibitors.
		+
		+	Crystal Structure of the Human Fatty Acid Synthase Enoyl-Acyl Carrier Protein-Reductase Domain Complexed with Triclosan Reveals Allosteric Protein-Protein Interface Inhibition.,Sippel KH, Vyas NK, Zhang W, Sankaran B, Quiocho FA J Biol Chem. 2014 Oct 9. pii: jbc.M114.608547. PMID:25301948<ref>PMID:25301948</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:06, 20 October 2014

OCA — Mon, 20 Oct 2014 11:06:52 GMT

←Older revision		Revision as of 11:06, 20 October 2014
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-	'''~~Unreleased structure~~'''	+	==Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan==
-		+	<StructureSection load='4w9n' size='340' side='right' caption='[[4w9n]], [[Resolution\|resolution]] 1.84Å' scene=''>
-	~~The entry~~ 4w9n is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4w9n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W9N FirstGlance]. <br>
-	~~Authors~~: ~~Sippel~~, K.H., ~~Vyas, N~~.K., ~~Sankaran, B~~., Quiocho, F.A.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>
-		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene></td></tr>
-	~~Description~~: Enoyl~~-acyl carrier protein-~~reductase ~~domain from human fatty~~ acid synthase ~~complexed with triclosan~~	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4w82\|4w82]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=4w9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w9n RCSB], [http://www.ebi.ac.uk/pdbsum/4w9n PDBsum]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Quiocho, F A.]]
		+	[[Category: Sankaran, B.]]
		+	[[Category: Sippel, K H.]]
		+	[[Category: Vyas, N K.]]
		+	[[Category: Enoyl reductase]]
		+	[[Category: Fatty acid metabolism]]
		+	[[Category: Fatty acid synthase]]
		+	[[Category: Nadph-dependent]]

OCA at 08:52, 10 September 2014

OCA — Wed, 10 Sep 2014 08:52:42 GMT

←Older revision		Revision as of 08:52, 10 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4w9n is ON HOLD	+	The entry 4w9n is ON HOLD until Paper Publication

	Authors: Sippel, K.H., Vyas, N.K., Sankaran, B., Quiocho, F.A.		Authors: Sippel, K.H., Vyas, N.K., Sankaran, B., Quiocho, F.A.

	Description: Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan		Description: Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan

OCA: Protected "4w9n" [edit=sysop:move=sysop]

OCA — Thu, 04 Sep 2014 04:50:43 GMT

Protected "4w9n" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:50, 4 September 2014