2vcy - Revision history

OCA at 15:15, 13 December 2023

OCA — Wed, 13 Dec 2023 15:15:44 GMT

←Older revision		Revision as of 15:15, 13 December 2023
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	<StructureSection load='2vcy' size='340' side='right'caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>		<StructureSection load='2vcy' size='340' side='right'caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vcy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VCY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vcy]] is a 2 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=2VCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VCY FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.41Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1zsy\|1zsy]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38]~~ </~~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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [https://pdbe.org/2vcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [https://www.ebi.ac.uk/pdbsum/2vcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcy 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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [https://pdbe.org/2vcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [https://www.ebi.ac.uk/pdbsum/2vcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcy ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/MECR_HUMAN MECR_HUMAN] Catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH-dependent manner with preference to medium chain length substrate. May have a role in the mitochondrial synthesis of fatty acids.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Haapalainen~~, A M~~]]	+	[[Category: Haapalainen AM]]
-	[[Category: Pudas, R]]	+	[[Category: Pudas R]]
-	[[Category: Smart~~, O S~~]]	+	[[Category: Smart OS]]
-	[[Category: Wierenga~~, R K]]~~	+	[[Category: Wierenga RK]]
-	~~[[Category: Enoyl thioester reductase]]~~	+
-	~~[[Category: Fatty acid biosynthesis]]~~	+
-	~~[[Category: Lipid synthesis]]~~	+
-	~~[[Category: Mitochondrion]]~~	+
-	~~[[Category: Nadp]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Transit peptide~~]]	+

OCA at 10:44, 7 July 2021

OCA — Wed, 07 Jul 2021 10:44:18 GMT

←Older revision		Revision as of 10:44, 7 July 2021
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	<StructureSection load='2vcy' size='340' side='right'caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>		<StructureSection load='2vcy' size='340' side='right'caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vcy]] is a 2 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=2VCY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VCY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vcy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VCY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1zsy\|1zsy]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zsy\|1zsy]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [~~http~~://pdbe.org/2vcy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vcy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcy 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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [https://pdbe.org/2vcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [https://www.ebi.ac.uk/pdbsum/2vcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcy ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==

OCA at 07:40, 24 July 2019

OCA — Wed, 24 Jul 2019 07:40:01 GMT

←Older revision		Revision as of 07:40, 24 July 2019
Line 1:		Line 1:

	==Crystal Structure of 2-Enoyl Thioester Reductase of Human FAS II==		==Crystal Structure of 2-Enoyl Thioester Reductase of Human FAS II==
-	<StructureSection load='2vcy' size='340' side='right' caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>	+	<StructureSection load='2vcy' size='340' side='right'caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vcy]] is a 2 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=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vcy]] is a 2 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=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Haapalainen, A M]]		[[Category: Haapalainen, A M]]
	[[Category: Pudas, R]]		[[Category: Pudas, R]]

OCA at 20:40, 19 September 2018

OCA — Wed, 19 Sep 2018 20:40:16 GMT

←Older revision		Revision as of 20:40, 19 September 2018
Line 1:		Line 1:

-	==~~CRYSTAL STRUCTURE OF~~ 2-~~ENOYL THIOESTER REDUCTASE OF HUMAN~~ FAS II==	+	==Crystal Structure of 2-Enoyl Thioester Reductase of Human FAS II==
	<StructureSection load='2vcy' size='340' side='right' caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>		<StructureSection load='2vcy' size='340' side='right' caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/2vcy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/2vcy_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 43:		Line 43:
	[[Category: Nadp]]		[[Category: Nadp]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
		+	[[Category: Polymorphism]]
	[[Category: Transit peptide]]		[[Category: Transit peptide]]

OCA at 07:21, 11 August 2016

OCA — Thu, 11 Aug 2016 07:21:09 GMT

←Older revision		Revision as of 07:21, 11 August 2016
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II==		==CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II==
	<StructureSection load='2vcy' size='340' side='right' caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>		<StructureSection load='2vcy' size='340' side='right' caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vcy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vcy]] is a 2 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=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1zsy\|1zsy]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1zsy\|1zsy]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [http://www.ebi.ac.uk/pdbsum/2vcy 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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [http://pdbe.org/2vcy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [http://www.ebi.ac.uk/pdbsum/2vcy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcy ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 16:		Line 17:
	<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=2vcy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		Line 27:
	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 2vcy" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Haapalainen, A M]]		[[Category: Haapalainen, A M]]
	[[Category: Pudas, R]]		[[Category: Pudas, R]]

OCA at 13:24, 19 January 2015

OCA — Mon, 19 Jan 2015 13:24:25 GMT

←Older revision		Revision as of 13:24, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vcy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vcy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1zsy\|1zsy]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1zsy\|1zsy]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [http://www.ebi.ac.uk/pdbsum/2vcy 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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [http://www.ebi.ac.uk/pdbsum/2vcy PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Haapalainen, A M.]]	+	[[Category: Haapalainen, A M]]
-	[[Category: Pudas, R.]]	+	[[Category: Pudas, R]]
-	[[Category: Smart, O S.]]	+	[[Category: Smart, O S]]
-	[[Category: Wierenga, R K.]]	+	[[Category: Wierenga, R K]]
	[[Category: Enoyl thioester reductase]]		[[Category: Enoyl thioester reductase]]
	[[Category: Fatty acid biosynthesis]]		[[Category: Fatty acid biosynthesis]]

OCA at 01:17, 1 October 2014

OCA — Wed, 01 Oct 2014 01:17:56 GMT

←Older revision		Revision as of 01:17, 1 October 2014
Line 1:		Line 1:
-	[[~~Image:~~2vcy.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II==
		+	<StructureSection load='2vcy' size='340' side='right' caption='[[2vcy]], [[Resolution\|resolution]] 2.41Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2vcy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VCY FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1zsy\|1zsy]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-2-enoyl-CoA_reductase_(NADPH) Trans-2-enoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.38 1.3.1.38] </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=2vcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vcy RCSB], [http://www.ebi.ac.uk/pdbsum/2vcy 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/vc/2vcy_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 ==
		+	Structural and kinetic properties of the human 2-enoyl thioester reductase [mitochondrial enoyl-coenzyme A reductase (MECR)/ETR1] of the mitochondrial fatty acid synthesis (FAS) II pathway have been determined. The crystal structure of this dimeric enzyme (at 2.4 A resolution) suggests that the binding site for the recognition helix of the acyl carrier protein is in a groove between the two adjacent monomers. This groove is connected via the pantetheine binding cleft to the active site. The modeled mode of NADPH binding, using molecular dynamics calculations, suggests that Tyr94 and Trp311 are critical for catalysis, which is supported by enzyme kinetic data. A deep, water-filled pocket, shaped by hydrophobic and polar residues and extending away from the catalytic site, was recognized. This pocket can accommodate a fatty acyl tail of up to 16 carbons. Mutagenesis of the residues near the end of this pocket confirms the importance of this region for the binding of substrate molecules with long fatty acyl tails. Furthermore, the kinetic analysis of the wild-type MECR/ETR1 shows a bimodal distribution of catalytic efficiencies, in agreement with the notion that two major products are generated by the mitochondrial FAS II pathway.

-	~~{{STRUCTURE_2vcy\| PDB=2vcy \| SCENE= }}~~	+	Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties.,Chen ZJ, Pudas R, Sharma S, Smart OS, Juffer AH, Hiltunen JK, Wierenga RK, Haapalainen AM J Mol Biol. 2008 Jun 13;379(4):830-44. Epub 2008 Apr 24. PMID:18479707<ref>PMID:18479707</ref>

-	~~===CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_18479707}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2vcy]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:018479707<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Haapalainen, A M.]]		[[Category: Haapalainen, A M.]]

OCA: Protected "2vcy" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 17:51:45 GMT

Protected "2vcy" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:51, 7 January 2013

OCA at 17:51, 7 January 2013

OCA — Mon, 07 Jan 2013 17:51:41 GMT

←Older revision		Revision as of 17:51, 7 January 2013
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-	{{Seed}}
	[[Image:2vcy.png\|left\|200px]]		[[Image:2vcy.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2vcy", 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),
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	{{STRUCTURE_2vcy\| PDB=2vcy \| SCENE= }}		{{STRUCTURE_2vcy\| PDB=2vcy \| SCENE= }}

	===CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II===		===CRYSTAL STRUCTURE OF 2-ENOYL THIOESTER REDUCTASE OF HUMAN FAS II===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18479707}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18479707 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18479707}}		{{ABSTRACT_PUBMED_18479707}}

	==About this Structure==		==About this Structure==
-	~~2VCY~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA].	+	[[2vcy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18479707~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018479707</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Haapalainen, A M.]]		[[Category: Haapalainen, A M.]]
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	[[Category: Nadp]]		[[Category: Nadp]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-	[[Category: Polymorphism]]
	[[Category: Transit peptide]]		[[Category: Transit peptide]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:57:33 2009''

OCA at 17:57, 17 February 2009

OCA — Tue, 17 Feb 2009 17:57:34 GMT

←Older revision		Revision as of 17:57, 17 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2VCY is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA].	+	2VCY is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VCY OCA].

	==Reference==		==Reference==
-	Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties., Chen ZJ, Pudas R, Sharma S, Smart OS, Juffer AH, Hiltunen JK, Wierenga RK, Haapalainen AM, J Mol Biol. 2008 Jun 13;379(4):830-44. Epub 2008 Apr 24. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18479707 18479707]~~	+	<ref group="xtra">PMID:18479707</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Haapalainen, A M.]]		[[Category: Haapalainen, A M.]]
	[[Category: Pudas, R.]]		[[Category: Pudas, R.]]
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	[[Category: Transit peptide]]		[[Category: Transit peptide]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue ~~Jul 29 03~~:51:~~27 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:57:33 2009''