3otq: Difference between revisions
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==Soluble Epoxide Hydrolase in complex with pyrazole antagonist== | ==Soluble Epoxide Hydrolase in complex with pyrazole antagonist== | ||
<StructureSection load='3otq' size='340' side='right'caption='[[3otq]]' scene=''> | <StructureSection load='3otq' size='340' side='right'caption='[[3otq]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OTQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[3otq]] 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=3OTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OTQ FirstGlance]. <br> | ||
</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=3otq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3otq OCA], [https://pdbe.org/3otq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3otq RCSB], [https://www.ebi.ac.uk/pdbsum/3otq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3otq ProSAT]</span></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]] 3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MZL:N-[4-(5-ETHYL-3-PYRIDIN-3-YL-1H-PYRAZOL-1-YL)PHENYL]PYRIDINE-3-CARBOXAMIDE'>MZL</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=3otq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3otq OCA], [https://pdbe.org/3otq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3otq RCSB], [https://www.ebi.ac.uk/pdbsum/3otq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3otq ProSAT]</span></td></tr> | |||
</table> | </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== | ==See Also== | ||
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] | *[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Farrow NA]] | [[Category: Farrow NA]] |
Latest revision as of 13:36, 21 February 2024
Soluble Epoxide Hydrolase in complex with pyrazole antagonistSoluble Epoxide Hydrolase in complex with pyrazole antagonist
Structural highlights
FunctionHYES_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.[1] [2] See AlsoReferences
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