4j03: Difference between revisions
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{{STRUCTURE_4j03| PDB=4j03 | SCENE= }} | |||
===Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant=== | |||
{{ABSTRACT_PUBMED_23684894}} | |||
The | ==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== | |||
[[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== | |||
<ref group="xtra">PMID:023684894</ref><references group="xtra"/><references/> | |||
[[Category: Homo sapiens]] | |||
[[Category: Hammock, B D.]] | |||
[[Category: Hwang, S H.]] | |||
[[Category: Morisseau, C.]] | |||
[[Category: Newcomer, M E.]] | |||
[[Category: Pakhomova, S.]] | |||
[[Category: Domain-swapped dimer]] | |||
[[Category: Hydrolase-hydrolase inhibitor complex]] | |||
Revision as of 08:15, 19 June 2013
Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant
Template:ABSTRACT PUBMED 23684894
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
4j03 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Morisseau C, Pakhomova S, Hwang SH, Newcomer ME, Hammock BD. Inhibition of soluble epoxide hydrolase by fulvestrant and sulfoxides. 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 doi:10.1016/j.bmcl.2013.04.083
- ↑ 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
