3pdc
From Proteopedia
m (Protected "3pdc" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | [[Image:3pdc.jpg|left|200px]] | ||
- | |||
- | <!-- | ||
- | The line below this paragraph, containing "STRUCTURE_3pdc", creates the "Structure Box" on the page. | ||
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
- | or leave the SCENE parameter empty for the default display. | ||
- | --> | ||
{{STRUCTURE_3pdc| PDB=3pdc | SCENE= }} | {{STRUCTURE_3pdc| PDB=3pdc | SCENE= }} | ||
- | |||
===Crystal structure of hydrolase domain of human soluble epoxide hydrolase complexed with a benzoxazole inhibitor=== | ===Crystal structure of hydrolase domain of human soluble epoxide hydrolase complexed with a benzoxazole inhibitor=== | ||
+ | {{ABSTRACT_PUBMED_21302953}} | ||
- | + | ==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> | |
- | + | ||
- | + | ||
- | --> | + | |
- | + | ||
==About this Structure== | ==About this Structure== | ||
Line 22: | Line 10: | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021302953</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Soluble epoxide hydrolase]] | [[Category: Soluble epoxide hydrolase]] | ||
[[Category: Kurumbail, R G.]] | [[Category: Kurumbail, R G.]] | ||
[[Category: Williams, J M.]] | [[Category: Williams, J M.]] | ||
+ | [[Category: Acetylation of lysine]] | ||
+ | [[Category: Alpha/beta hydrolase fold]] | ||
+ | [[Category: Beta barrel]] | ||
+ | [[Category: Binds mg2+]] | ||
+ | [[Category: Cytoplasm]] | ||
+ | [[Category: Epoxide hydrolase]] | ||
+ | [[Category: Epoxide hydrolase fold]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
+ | [[Category: Hypertension]] | ||
+ | [[Category: Peroxisome]] |
Revision as of 08:38, 2 May 2013
Contents |
Crystal structure of hydrolase domain of human soluble epoxide hydrolase complexed with a benzoxazole inhibitor
Template:ABSTRACT PUBMED 21302953
Function
[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 Structure
3pdc is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Xing L, McDonald JJ, Kolodziej SA, Kurumbail RG, Williams JM, Warren CJ, O'Neal JM, Skepner JE, Roberds SL. Discovery of potent inhibitors of soluble epoxide hydrolase by combinatorial library design and structure-based virtual screening. J Med Chem. 2011 Mar 10;54(5):1211-22. Epub 2011 Feb 8. PMID:21302953 doi:10.1021/jm101382t
- ↑ 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
- ↑ 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
Categories: Homo sapiens | Soluble epoxide hydrolase | Kurumbail, R G. | Williams, J M. | Acetylation of lysine | Alpha/beta hydrolase fold | Beta barrel | Binds mg2+ | Cytoplasm | Epoxide hydrolase | Epoxide hydrolase fold | Hydrolase | Hydrolase-hydrolase inhibitor complex | Hypertension | Peroxisome