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==Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant==
==Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant==
<StructureSection load='4j03' size='340' side='right' caption='[[4j03]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
<StructureSection load='4j03' size='340' side='right'caption='[[4j03]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4j03]] 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=4J03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J03 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4j03]] 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=4J03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J03 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FVS:(7BETA,9BETA,13ALPHA,17BETA)-7-{9-[(R)-(4,4,5,5,5-PENTAFLUOROPENTYL)SULFINYL]NONYL}ESTRA-1(10),2,4-TRIENE-3,17-DIOL'>FVS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.92&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FVS:(7BETA,9BETA,13ALPHA,17BETA)-7-{9-[(R)-(4,4,5,5,5-PENTAFLUOROPENTYL)SULFINYL]NONYL}ESTRA-1(10),2,4-TRIENE-3,17-DIOL'>FVS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j03 OCA], [http://pdbe.org/4j03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j03 RCSB], [http://www.ebi.ac.uk/pdbsum/4j03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j03 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=4j03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j03 OCA], [https://pdbe.org/4j03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j03 RCSB], [https://www.ebi.ac.uk/pdbsum/4j03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j03 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>  
<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==
*[[Epoxide hydrolase|Epoxide hydrolase]]
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Hammock, B D]]
[[Category: Large Structures]]
[[Category: Hwang, S H]]
[[Category: Hammock BD]]
[[Category: Morisseau, C]]
[[Category: Hwang SH]]
[[Category: Newcomer, M E]]
[[Category: Morisseau C]]
[[Category: Pakhomova, S]]
[[Category: Newcomer ME]]
[[Category: Domain-swapped dimer]]
[[Category: Pakhomova S]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

Latest revision as of 15:34, 20 September 2023

Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant

4j03, resolution 2.92Å

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