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4x6y

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==Human soluble epoxide hydrolase in complex with a cyclopropyl urea derivative==
==Human soluble epoxide hydrolase in complex with a cyclopropyl urea derivative==
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<StructureSection load='4x6y' size='340' side='right' caption='[[4x6y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='4x6y' size='340' side='right'caption='[[4x6y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4x6y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X6Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4x6y]] 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=4X6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X6Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=S94:4-PHENOXY-N-[(1S,2R)-2-PHENYLCYCLOPROPYL]PIPERIDINE-1-CARBOXAMIDE'>S94</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x6x|4x6x]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=S94:4-PHENOXY-N-[(1S,2R)-2-PHENYLCYCLOPROPYL]PIPERIDINE-1-CARBOXAMIDE'>S94</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Soluble_epoxide_hydrolase Soluble epoxide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.10 3.3.2.10] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6y OCA], [https://pdbe.org/4x6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x6y RCSB], [https://www.ebi.ac.uk/pdbsum/4x6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6y ProSAT]</span></td></tr>
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<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=4x6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6y OCA], [http://pdbe.org/4x6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x6y RCSB], [http://www.ebi.ac.uk/pdbsum/4x6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6y ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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==
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*[[Epoxide hydrolase|Epoxide hydrolase]]
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*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Soluble epoxide hydrolase]]
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[[Category: Homo sapiens]]
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[[Category: Chiyo, N]]
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[[Category: Large Structures]]
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[[Category: Ishii, T]]
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[[Category: Chiyo N]]
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[[Category: Takai, K]]
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[[Category: Ishii T]]
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[[Category: Hydrolase]]
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[[Category: Takai K]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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Current revision

Human soluble epoxide hydrolase in complex with a cyclopropyl urea derivative

PDB ID 4x6y

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