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4y2s
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of soluble epoxide hydrolase in complex with 1-[3-(trifluoromethyl)phenyl]-1H-pyrazol-4-ol== | |
| + | <StructureSection load='4y2s' size='340' side='right'caption='[[4y2s]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4y2s]] 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=4Y2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y2S FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=49P:1-[3-(TRIFLUOROMETHYL)PHENYL]-1H-PYRAZOL-4-OL'>49P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4y2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y2s OCA], [https://pdbe.org/4y2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y2s RCSB], [https://www.ebi.ac.uk/pdbsum/4y2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y2s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| - | + | ==See Also== | |
| - | + | *[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Amano | + | __TOC__ |
| - | [[Category: Yamaguchi | + | </StructureSection> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Amano Y]] | ||
| + | [[Category: Yamaguchi T]] | ||
Current revision
Structure of soluble epoxide hydrolase in complex with 1-[3-(trifluoromethyl)phenyl]-1H-pyrazol-4-ol
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