8qvi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "8qvi" [edit=sysop:move=sysop])
Current revision (10:08, 17 January 2024) (edit) (undo)
 
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 8qvi is ON HOLD
+
==Comparison of room-temperature and cryogenic structures of soluble Epoxide Hydrolase with ligands bound.==
-
 
+
<StructureSection load='8qvi' size='340' side='right'caption='[[8qvi]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[8qvi]] 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=8QVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QVI FirstGlance]. <br>
-
Description:
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8qvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qvi OCA], [https://pdbe.org/8qvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qvi RCSB], [https://www.ebi.ac.uk/pdbsum/8qvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qvi 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>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Bjelcic M]]
 +
[[Category: Branden G]]
 +
[[Category: Dunge A]]
 +
[[Category: Gunnarsson J]]
 +
[[Category: Kack H]]
 +
[[Category: Phan C]]
 +
[[Category: Uwangue O]]
 +
[[Category: Wehlander G]]

Current revision

Comparison of room-temperature and cryogenic structures of soluble Epoxide Hydrolase with ligands bound.

PDB ID 8qvi

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/8qvi"
Personal tools