8s77: Difference between revisions
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==Soluble epoxide hydrolase in complex with PROTAC JSF234== | |||
<StructureSection load='8s77' size='340' side='right'caption='[[8s77]], [[Resolution|resolution]] 1.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8s77]] 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=8S77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8S77 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]] 1.36Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1H5J:~{N}-[[4-(cyclopropylsulfonylamino)-2-(trifluoromethyl)phenyl]methyl]-1-ethylsulfonyl-indole-5-carboxamide'>A1H5J</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8s77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8s77 OCA], [https://pdbe.org/8s77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8s77 RCSB], [https://www.ebi.ac.uk/pdbsum/8s77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8s77 ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: Knapp | == Function == | ||
[[Category: | [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> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Schoenfeld | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Hiesinger K]] | |||
[[Category: Knapp S]] | |||
[[Category: Kumar A]] | |||
[[Category: Lillich F]] | |||
[[Category: Proschak E]] | |||
[[Category: Schoenfeld J]] | |||