3fcx - Revision history

OCA at 15:28, 1 November 2023

2023-11-01T15:28:43Z

←Older revision		Revision as of 15:28, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3fcx' size='340' side='right'caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3fcx' size='340' side='right'caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCX FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.5Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ESD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12]~~ </~~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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [https://pdbe.org/3fcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [https://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx 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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [https://pdbe.org/3fcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [https://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN]] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref>	+	[https://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: S-formylglutathione hydrolase]]~~	+	[[Category: Li Y]]
-	[[Category: Li, Y]]	+	[[Category: Liu ZJ]]
-	[[Category: Liu~~, Z J~~]]	+	[[Category: Shaw N]]
-	[[Category: Shaw, N]]	+	[[Category: Song G]]
-	[[Category: Song, G]]	+	[[Category: Wu D]]
-	[[Category: Wu, D]]	+	[[Category: Zhang D]]
-	[[Category: Zhang, D]]	+
-	~~[[Category: Cytoplasm]]~~	+
-	~~[[Category: Cytoplasmic vesicle]]~~	+
-	~~[[Category: Esterase]]~~	+
-	~~[[Category: Genetic marker]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Retinoblastoma]]~~	+
-	~~[[Category: Serine esterase~~]]	+

OCA at 07:38, 10 November 2021

2021-11-10T07:38:48Z

←Older revision		Revision as of 07:38, 10 November 2021
Line 1:		Line 1:

	==Crystal structure of human esterase D==		==Crystal structure of human esterase D==
-	<StructureSection load='3fcx' size='340' side='right' caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='3fcx' size='340' side='right'caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3FCX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCX FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([https://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/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [~~http~~://pdbe.org/3fcx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx 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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [https://pdbe.org/3fcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [https://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN]] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref>	+	[[https://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN]] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: S-formylglutathione hydrolase]]		[[Category: S-formylglutathione hydrolase]]
	[[Category: Li, Y]]		[[Category: Li, Y]]

OCA at 07:52, 5 December 2018

2018-12-05T07:52:25Z

←Older revision		Revision as of 07:52, 5 December 2018
Line 1:		Line 1:
		+
	==Crystal structure of human esterase D==		==Crystal structure of human esterase D==
	<StructureSection load='3fcx' size='340' side='right' caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3fcx' size='340' side='right' caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([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/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://pdbe.org/3fcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx 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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://pdbe.org/3fcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/3fcx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/3fcx_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 41:		Line 42:
	[[Category: Wu, D]]		[[Category: Wu, D]]
	[[Category: Zhang, D]]		[[Category: Zhang, D]]
		+	[[Category: Cytoplasm]]
	[[Category: Cytoplasmic vesicle]]		[[Category: Cytoplasmic vesicle]]
	[[Category: Esterase]]		[[Category: Esterase]]
	[[Category: Genetic marker]]		[[Category: Genetic marker]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
		+	[[Category: Polymorphism]]
	[[Category: Retinoblastoma]]		[[Category: Retinoblastoma]]
	[[Category: Serine esterase]]		[[Category: Serine esterase]]

OCA at 15:28, 9 February 2016

2016-02-09T15:28:24Z

←Older revision		Revision as of 15:28, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='3fcx' size='340' side='right' caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3fcx' size='340' side='right' caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FCX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FCX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([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/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx 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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://pdbe.org/3fcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<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=3fcx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	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 3fcx" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: S-formylglutathione hydrolase]]		[[Category: S-formylglutathione hydrolase]]
	[[Category: Li, Y]]		[[Category: Li, Y]]

OCA at 07:43, 25 December 2014

2014-12-25T07:43:50Z

←Older revision		Revision as of 07:43, 25 December 2014
Line 8:		Line 8:
	<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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx 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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ESTD_HUMAN ESTD_HUMAN]] Serine hydrolase involved in the detoxification of formaldehyde.<ref>PMID:4768551</ref> <ref>PMID:3770744</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:42, 26 November 2014

2014-11-26T08:42:56Z

←Older revision		Revision as of 08:42, 26 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3fcx.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of human esterase D==
		+	<StructureSection load='3fcx' size='340' side='right' caption='[[3fcx]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3fcx]] 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=3FCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FCX FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ESD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/S-formylglutathione_hydrolase S-formylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.12 3.1.2.12] </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=3fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fcx RCSB], [http://www.ebi.ac.uk/pdbsum/3fcx 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/fc/3fcx_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 ==
		+	Retinoblastoma (RB), a carcinoma of the retina, is caused by mutations in the long arm of chromosome 13, band 13q14. The esterase D (ESD) gene maps at a similar location as the RB gene locus and therefore serves as a potential marker for the prognosis of retinoblastoma. Because very little is known about the structure and function of ESD, we determined the 3-dimensional structure of the enzyme at 1.5 A resolution using X-ray crystallography. ESD shows a single domain with an alpha/beta-hydrolase fold. A number of insertions are observed in the canonical alpha/beta-hydrolase fold. The active site is located in a positively charged, shallow cleft on the surface lined by a number of aromatic residues. Superimposition studies helped identify the typical catalytic triad residues--Ser-153, His264, and Asp230--involved in catalysis. Mutagenesis of any of the catalytic triad residues to alanine abolished the enzyme activity. Backbone amides of Leu54 and Met150 are involved in the formation of the oxyanion hole. Interestingly, a M150A mutation increased the enzyme activity by 62%. The structure of human ESD determined in this study will aid the elucidation of the physiological role of the enzyme in the human body and will assist in the early diagnosis of retinoblastoma.

-	~~{{STRUCTURE_3fcx\| PDB=3fcx \| SCENE= }}~~	+	Crystal structure of human esterase D: a potential genetic marker of retinoblastoma.,Wu D, Li Y, Song G, Zhang D, Shaw N, Liu ZJ FASEB J. 2009 May;23(5):1441-6. Epub 2009 Jan 6. PMID:19126594<ref>PMID:19126594</ref>

-	~~===Crystal structure~~ of ~~human esterase D===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_19126594}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[3fcx]] 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=3FCX OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:019126594<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: S-formylglutathione hydrolase]]		[[Category: S-formylglutathione hydrolase]]
-	[[Category: Li, Y.]]	+	[[Category: Li, Y]]
-	[[Category: Liu, Z J.]]	+	[[Category: Liu, Z J]]
-	[[Category: Shaw, N.]]	+	[[Category: Shaw, N]]
-	[[Category: Song, G.]]	+	[[Category: Song, G]]
-	[[Category: Wu, D.]]	+	[[Category: Wu, D]]
-	[[Category: Zhang, D.]]	+	[[Category: Zhang, D]]
	[[Category: Cytoplasmic vesicle]]		[[Category: Cytoplasmic vesicle]]
	[[Category: Esterase]]		[[Category: Esterase]]

OCA: Protected "3fcx" [edit=sysop:move=sysop]

2013-02-13T11:01:49Z

Protected "3fcx" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:01, 13 February 2013

OCA at 11:01, 13 February 2013

2013-02-13T11:01:46Z

←Older revision		Revision as of 11:01, 13 February 2013
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	[[Image:3fcx.png\|left\|200px]]		[[Image:3fcx.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3fcx\| PDB=3fcx \| SCENE= }}		{{STRUCTURE_3fcx\| PDB=3fcx \| SCENE= }}

	===Crystal structure of human esterase D===		===Crystal structure of human esterase D===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19126594}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19126594 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_19126594}}		{{ABSTRACT_PUBMED_19126594}}

	==About this Structure==		==About this Structure==
-	~~3FCX~~ 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=3FCX OCA].	+	[[3fcx]] 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=3FCX OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19126594~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019126594</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: S-formylglutathione hydrolase]]		[[Category: S-formylglutathione hydrolase]]
Line 32:		Line 20:
	[[Category: Wu, D.]]		[[Category: Wu, D.]]
	[[Category: Zhang, D.]]		[[Category: Zhang, D.]]
-	[[Category: Cytoplasm]]
	[[Category: Cytoplasmic vesicle]]		[[Category: Cytoplasmic vesicle]]
	[[Category: Esterase]]		[[Category: Esterase]]
	[[Category: Genetic marker]]		[[Category: Genetic marker]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
-	[[Category: Polymorphism]]
	[[Category: Retinoblastoma]]		[[Category: Retinoblastoma]]
	[[Category: Serine esterase]]		[[Category: Serine esterase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 13 10:09:24 2009''

OCA at 07:09, 13 May 2009

2009-05-13T07:09:25Z

←Older revision		Revision as of 07:09, 13 May 2009
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	{{Seed}}		{{Seed}}
-	[[Image:3fcx.~~jpg~~\|left\|200px]]	+	[[Image:3fcx.png\|left\|200px]]

	<!--		<!--
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	===Crystal structure of human esterase D===		===Crystal structure of human esterase D===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19126594}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19126594 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19126594}}

	==About this Structure==		==About this Structure==
	3FCX 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=3FCX OCA].		3FCX 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=3FCX OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:19126594</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: S-formylglutathione hydrolase]]		[[Category: S-formylglutathione hydrolase]]
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	[[Category: Serine esterase]]		[[Category: Serine esterase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Dec~~ 10 15:11:~~10 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 13 10:09:24 2009''

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