4c4z

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==Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A8==
==Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A8==
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<StructureSection load='4c4z' size='340' side='right' caption='[[4c4z]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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<StructureSection load='4c4z' size='340' side='right'caption='[[4c4z]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c4z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C4Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c4z]] 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=4C4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C4Z 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=W9L:1-ETHYL-3-NAPHTHALEN-1-YLUREA'>W9L</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]] 2.06&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c4x|4c4x]], [[4c4y|4c4y]]</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=W9L:1-ETHYL-3-NAPHTHALEN-1-YLUREA'>W9L</scene></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=4c4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c4z RCSB], [http://www.ebi.ac.uk/pdbsum/4c4z PDBsum]</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=4c4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c4z OCA], [https://pdbe.org/4c4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c4z RCSB], [https://www.ebi.ac.uk/pdbsum/4c4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c4z ProSAT]</span></td></tr>
</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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4c4z" style="background-color:#fffaf0;"></div>
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==See Also==
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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: Becker, S]]
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[[Category: Homo sapiens]]
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[[Category: Elshorst, B]]
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[[Category: Large Structures]]
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[[Category: Griesinger, C]]
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[[Category: Becker S]]
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[[Category: Hessler, G]]
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[[Category: Elshorst B]]
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[[Category: Krimm, I]]
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[[Category: Griesinger C]]
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[[Category: Langer, T]]
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[[Category: Hessler G]]
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[[Category: Lee, D]]
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[[Category: Krimm I]]
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[[Category: Mazur, A]]
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[[Category: Langer T]]
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[[Category: Monecke, P]]
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[[Category: Lee D]]
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[[Category: Pilger, J]]
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[[Category: Mazur A]]
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[[Category: Schiffer, A]]
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[[Category: Monecke P]]
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[[Category: Schreuder, H]]
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[[Category: Pilger J]]
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[[Category: Wegstroth, M]]
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[[Category: Schiffer A]]
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[[Category: Wendt, K U]]
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[[Category: Schreuder H]]
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[[Category: Drug design]]
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[[Category: Wegstroth M]]
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[[Category: Hydrolase]]
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[[Category: Wendt K-U]]
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[[Category: Multiple binding mode]]
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Current revision

Crystal structure of human bifunctional epoxide hydroxylase 2 complexed with A8

PDB ID 4c4z

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