4j03

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:34, 20 September 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_4j03| PDB=4j03 | SCENE= }}
 
-
===Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant===
 
-
{{ABSTRACT_PUBMED_23684894}}
 
-
==Function==
+
==Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant==
-
[[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>
+
<StructureSection load='4j03' size='340' side='right'caption='[[4j03]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4j03]] 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=4J03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J03 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]] 2.92&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FVS:(7BETA,9BETA,13ALPHA,17BETA)-7-{9-[(R)-(4,4,5,5,5-PENTAFLUOROPENTYL)SULFINYL]NONYL}ESTRA-1(10),2,4-TRIENE-3,17-DIOL'>FVS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4j03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j03 OCA], [https://pdbe.org/4j03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j03 RCSB], [https://www.ebi.ac.uk/pdbsum/4j03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j03 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>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The soluble epoxide hydrolase (sEH) is a key enzyme in the metabolism of epoxy-fatty acids, signaling molecules involved in numerous biologies. Toward finding novel inhibitors of sEH, a library of known drugs was tested for inhibition of sEH. We found that fulvestrant, an anticancer agent, is a potent (KI=26nM) competitive inhibitor of sEH. From this observation, we found that alkyl-sulfoxides represent a new kind of pharmacophore for the inhibition of sEH.
-
==About this Structure==
+
Inhibition of soluble epoxide hydrolase by fulvestrant and sulfoxides.,Morisseau C, Pakhomova S, Hwang SH, Newcomer ME, Hammock BD Bioorg Med Chem Lett. 2013 Jul 1;23(13):3818-21. doi: 10.1016/j.bmcl.2013.04.083., Epub 2013 May 6. PMID:23684894<ref>PMID:23684894</ref>
-
[[4j03]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J03 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:023684894</ref><references group="xtra"/><references/>
+
</div>
 +
<div class="pdbe-citations 4j03" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Hammock, B D.]]
+
[[Category: Large Structures]]
-
[[Category: Hwang, S H.]]
+
[[Category: Hammock BD]]
-
[[Category: Morisseau, C.]]
+
[[Category: Hwang SH]]
-
[[Category: Newcomer, M E.]]
+
[[Category: Morisseau C]]
-
[[Category: Pakhomova, S.]]
+
[[Category: Newcomer ME]]
-
[[Category: Domain-swapped dimer]]
+
[[Category: Pakhomova S]]
-
[[Category: Hydrolase-hydrolase inhibitor complex]]
+

Current revision

Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant

PDB ID 4j03

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4j03"
Personal tools