4jnc
From Proteopedia
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==Soluble Epoxide Hydrolase complexed with a carboxamide inhibitor== | ==Soluble Epoxide Hydrolase complexed with a carboxamide inhibitor== | ||
- | <StructureSection load='4jnc' size='340' side='right' caption='[[4jnc]], [[Resolution|resolution]] 1.96Å' scene=''> | + | <StructureSection load='4jnc' size='340' side='right'caption='[[4jnc]], [[Resolution|resolution]] 1.96Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4jnc]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4jnc]] 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=4JNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JNC FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1LF:1-[4-METHYL-6-(METHYLAMINO)-1,3,5-TRIAZIN-2-YL]-N-[2-(TRIFLUOROMETHYL)BENZYL]PIPERIDINE-4-CARBOXAMIDE'>1LF</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1LF:1-[4-METHYL-6-(METHYLAMINO)-1,3,5-TRIAZIN-2-YL]-N-[2-(TRIFLUOROMETHYL)BENZYL]PIPERIDINE-4-CARBOXAMIDE'>1LF</scene></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jnc OCA], [https://pdbe.org/4jnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jnc RCSB], [https://www.ebi.ac.uk/pdbsum/4jnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jnc ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 4jnc" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Shewchuk LM]] |
- | + |
Current revision
Soluble Epoxide Hydrolase complexed with a carboxamide inhibitor
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