3wkc: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_3wkc|  PDB=3wkc  |  SCENE=  }}
===Crystal structure of soluble epoxide hydrolase in complex with fragment inhibitor===
{{ABSTRACT_PUBMED_24656800}}


The entry 3wkc is ON HOLD
==Function==
[[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> 


Authors: Amano, Y., Yamaguchi, T., Tanabe, E.
==About this Structure==
[[3wkc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WKC OCA].  


Description: Crystal structure of soluble epoxide hydrolase in complex with fragment inhibitor
==Reference==
<ref group="xtra">PMID:024656800</ref><references group="xtra"/><references/>
[[Category: Amano, Y.]]
[[Category: Tanabe, E.]]
[[Category: Yamaguchi, T.]]
[[Category: Hydrolase]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 12:44, 16 April 2014

Template:STRUCTURE 3wkc

Crystal structure of soluble epoxide hydrolase in complex with fragment inhibitorCrystal structure of soluble epoxide hydrolase in complex with fragment inhibitor

Template:ABSTRACT PUBMED 24656800

FunctionFunction

[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.[1] [2]

About this StructureAbout this Structure

3wkc is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Amano Y, Yamaguchi T, Tanabe E. Structural insights into binding of inhibitors to soluble epoxide hydrolase gained by fragment screening and X-ray crystallography. Bioorg Med Chem. 2014 Apr 15;22(8):2427-34. doi: 10.1016/j.bmc.2014.03.001. Epub , 2014 Mar 12. PMID:24656800 doi:http://dx.doi.org/10.1016/j.bmc.2014.03.001
  1. Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1552-7. Epub 2003 Feb 6. PMID:12574508 doi:10.1073/pnas.0437829100
  2. Newman JW, Morisseau C, Harris TR, Hammock BD. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1558-63. Epub 2003 Feb 6. PMID:12574510 doi:10.1073/pnas.0437724100

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