1zd2 - Revision history

OCA at 07:07, 23 August 2023

OCA — Wed, 23 Aug 2023 07:07:33 GMT

←Older revision		Revision as of 07:07, 23 August 2023
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	<StructureSection load='1zd2' size='340' side='right'caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1zd2' size='340' side='right'caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>~~, ~~<scene name='pdbligand=NC3:N-~~[~~(CYCLOHEXYLAMINO)CARBONYL~~]~~GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 3Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>~~[~~[Gene\|Gene:]]</b></td><td class="sblockDat">EPHX2~~ (~~[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN~~]~~)</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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [https://pdbe.org/1zd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [https://www.ebi.ac.uk/pdbsum/1zd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zd2 ProSAT]</span></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10]~~ </~~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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [~~http~~://pdbe.org/1zd2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1zd2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1zd2 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN]] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref>	+	[https://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Hydrolase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Christianson~~, D W~~]]	+	[[Category: Christianson DW]]
-	[[Category: Gomez~~, G A~~]]	+	[[Category: Gomez GA]]
-	[[Category: Hammock~~, B D~~]]	+	[[Category: Hammock BD]]
-	[[Category: Morisseau, C]]	+	[[Category: Morisseau C]]
-	~~[[Category: Domain-swapped dimer~~]]	+

OCA at 09:02, 20 January 2021

OCA — Wed, 20 Jan 2021 09:02:24 GMT

←Older revision		Revision as of 09:02, 20 January 2021
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	==Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex==		==Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex==
-	<StructureSection load='1zd2' size='340' side='right' caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='1zd2' size='340' side='right'caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPHX2 ([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">EPHX2 ([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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://pdbe.org/1zd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zd2 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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://pdbe.org/1zd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zd2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 1zd2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1zd2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Epoxide hydrolase 3D structures\|Epoxide hydrolase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 40:
	[[Category: Human]]		[[Category: Human]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
		+	[[Category: Large Structures]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]
	[[Category: Gomez, G A]]		[[Category: Gomez, G A]]

OCA at 09:21, 2 May 2018

OCA — Wed, 02 May 2018 09:21:20 GMT

←Older revision		Revision as of 09:21, 2 May 2018
Line 1:		Line 1:
		+
	==Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex==		==Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex==
	<StructureSection load='1zd2' size='340' side='right' caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1zd2' size='340' side='right' caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPHX2 ([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">EPHX2 ([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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://pdbe.org/1zd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://pdbe.org/1zd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zd2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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/zd/1zd2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zd/1zd2_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 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1zd2" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1zd2" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Epoxide hydrolase\|Epoxide hydrolase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:17, 9 February 2016

OCA — Tue, 09 Feb 2016 10:17:02 GMT

←Older revision		Revision as of 10:17, 9 February 2016
Line 19:		Line 19:
	<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=1zd2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:16, 10 September 2015

OCA — Thu, 10 Sep 2015 21:16:29 GMT

←Older revision		Revision as of 21:16, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1zd2' size='340' side='right' caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1zd2' size='340' side='right' caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPHX2 ([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">EPHX2 ([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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://pdbe.org/1zd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1zd2" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Epoxide hydrolase\|Epoxide hydrolase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Christianson, D W]]		[[Category: Christianson, D W]]

OCA at 06:12, 25 December 2014

OCA — Thu, 25 Dec 2014 06:12:27 GMT

←Older revision		Revision as of 06:12, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPHX2 ([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">EPHX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN]] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
-	[[Category: Christianson, D W.]]	+	[[Category: Christianson, D W]]
-	[[Category: Gomez, G A.]]	+	[[Category: Gomez, G A]]
-	[[Category: Hammock, B D.]]	+	[[Category: Hammock, B D]]
-	[[Category: Morisseau, C.]]	+	[[Category: Morisseau, C]]
	[[Category: Domain-swapped dimer]]		[[Category: Domain-swapped dimer]]
-	[[Category: Hydrolase]]

OCA at 21:37, 29 September 2014

OCA — Mon, 29 Sep 2014 21:37:52 GMT

←Older revision		Revision as of 21:37, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1zd2.~~png~~\|~~left~~\|200px]]	+	==Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex==
		+	<StructureSection load='1zd2' size='340' side='right' caption='[[1zd2]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1zd2]] is a 1 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=1ZD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZD2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NC3:N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE'>NC3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1s8o\|1s8o]], [[1vj5\|1vj5]], [[1zd3\|1zd3]], [[1zd4\|1zd4]], [[1zd5\|1zd5]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPHX2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 and 3.3.2.10 3.3.2.9 and 3.3.2.10] </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=1zd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zd2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zd2 RCSB], [http://www.ebi.ac.uk/pdbsum/1zd2 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/zd/1zd2_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 ==
		+	X-ray crystal structures of human soluble epoxide hydrolase (sEH) complexed with four different dialkylurea inhibitors bearing pendant carboxylate "tails" of varying length have been determined at 2.3-3.0 A resolution. Similarities among inhibitor binding modes reinforce the proposed roles of Y381 and/or Y465 as general acids that protonate the epoxide ring of the substrate in concert with nucleophilic attack of D333 at the electrophilic epoxide carbon. Additionally, the binding of these inhibitors allows us to model the binding mode of the endogenous substrate 14,15-epoxyeicosatrienoic acid. Contrasts among inhibitor binding modes include opposite orientations of inhibitor binding in the active-site hydrophobic tunnel. Alternative binding orientations observed for this series of inhibitors to human sEH, as well as the binding of certain dialkylurea inhibitors to human sEH and murine sEH, complicate the structure-based design of human sEH inhibitors with potential pharmaceutical applications in the treatment of hypertension. Thus, with regard to the optimization of inhibitor designs targeting human sEH, it is critical that human sEH and not murine sEH be utilized for inhibitor screening, and it is critical that structures of human sEH-inhibitor complexes be determined to verify inhibitor binding orientations that correlate with measured affinities.

-	~~{{STRUCTURE_1zd2\| PDB=1zd2 \| SCENE= }}~~	+	Human soluble epoxide hydrolase: structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids.,Gomez GA, Morisseau C, Hammock BD, Christianson DW Protein Sci. 2006 Jan;15(1):58-64. Epub 2005 Dec 1. PMID:16322563<ref>PMID:16322563</ref>

-	~~===Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16322563}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1zd2]] is~~ a ~~1 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=1ZD2 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016322563<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA: Protected "1zd2" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 17:44:31 GMT

Protected "1zd2" [edit=sysop:move=sysop]

←Older revision

Revision as of 17:44, 5 January 2013

OCA at 17:44, 5 January 2013

OCA — Sat, 05 Jan 2013 17:44:27 GMT

←Older revision		Revision as of 17:44, 5 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1zd2.png\|left\|200px]]		[[Image:1zd2.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1zd2", 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),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1zd2\| PDB=1zd2 \| SCENE= }}		{{STRUCTURE_1zd2\| PDB=1zd2 \| SCENE= }}

	===Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex===		===Human soluble epoxide hydrolase 4-(3-cyclohexyluriedo)-ethanoic acid complex===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16322563}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16322563 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16322563}}		{{ABSTRACT_PUBMED_16322563}}
-
-	==Disease==
-	Known disease associated with this structure: Hypercholesterolemia, familial, due to LDLR defect, modifier of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=132811 132811]]

	==About this Structure==		==About this Structure==
-	~~1ZD2~~ is a 1 chain 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=1ZD2 OCA].	+	[[1zd2]] is a 1 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=1ZD2 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16322563~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016322563</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: ~~Microsomal epoxide hydrolase~~]]	+	[[Category: Hydrolase]]
	[[Category: Christianson, D W.]]		[[Category: Christianson, D W.]]
	[[Category: Gomez, G A.]]		[[Category: Gomez, G A.]]
Line 34:		Line 19:
	[[Category: Morisseau, C.]]		[[Category: Morisseau, C.]]
	[[Category: Domain-swapped dimer]]		[[Category: Domain-swapped dimer]]
-		+	[[Category: Hydrolase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 09:04:23 2009''~~	+

OCA at 07:04, 17 February 2009

OCA — Tue, 17 Feb 2009 07:04:24 GMT

←Older revision		Revision as of 07:04, 17 February 2009
Line 23:		Line 23:

	==About this Structure==		==About this Structure==
-	1ZD2 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=1ZD2 OCA].	+	1ZD2 is a 1 chain 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=1ZD2 OCA].

	==Reference==		==Reference==
-	Human soluble epoxide hydrolase: structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids., Gomez GA, Morisseau C, Hammock BD, Christianson DW, Protein Sci. 2006 Jan;15(1):58-64. Epub 2005 Dec 1. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16322563 16322563]~~	+	<ref group="xtra">PMID:16322563</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Microsomal epoxide hydrolase]]		[[Category: Microsomal epoxide hydrolase]]
-	[[Category: Single protein]]
	[[Category: Christianson, D W.]]		[[Category: Christianson, D W.]]
	[[Category: Gomez, G A.]]		[[Category: Gomez, G A.]]
Line 36:		Line 35:
	[[Category: Domain-swapped dimer]]		[[Category: Domain-swapped dimer]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28 12~~:33:~~16 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:04:23 2009''