Sandbox Reserved 714

(Difference between revisions)

Revision as of 18:38, 30 December 2012

X-ray crystal structure of hsEH: assymetric unit, 1s8o

Ligands:

Gene:

EPHX2 (Homo sapiens)

Activity:

Hydrolase, with EC number and 3.3.2.10 3.3.2.9 and 3.3.2.10

Related:

1vj5

Structural annotation:
Resources:	InterPro : Ipr011945, Ipr005834, Ipr006402, Ipr003089, Ipr005833, Ipr000639, Ipr000073 Pfam : PF00702, PF00561 SCOP : d1s8oa2, d1s8oa1 UniProt : P34913

Functional annotation:
Cellular component:	peroxisome soluble fraction cytosol cytoplasm
Biological process:	oxygen and reactive oxygen species metabolic process cellular calcium ion homeostasis inflammatory response response to toxin metabolic process positive regulation of vasodilation xenobiotic metabolic process drug metabolic process aromatic compound metabolic process aromatic compound catabolic process regulation of blood pressure
Molecular function:	magnesium ion binding catalytic activity epoxide hydrolase activity metal ion binding hydrolase activity protein homodimerization activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

Human Soluble Epoxide Hydrolase: Biological assembly, 1s8o

The Human soluble Epoxide hydrolase is a homodimer. Each subunit has , linked by a proline-rich section.

DUTREUX Fabien, BONHOURE Anna

Revision as of 17:43, 30 December 2012 (edit) Anna Bonhoure (Talk \| contribs) ← Previous diff		Revision as of 18:38, 30 December 2012 (edit) (undo) Anna Bonhoure (Talk \| contribs) Next diff →
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	<Structure load='1s8o_mm1.pdb' size='400' frame='true' align='left' caption='X-ray crystal structure of hsEH' scene='Insert optional scene name here' />		<Structure load='1s8o_mm1.pdb' size='400' frame='true' align='left' caption='X-ray crystal structure of hsEH' scene='Insert optional scene name here' />
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		+	The Human soluble Epoxide hydrolase is a homodimer. Each subunit has <scene name='Sandbox_Reserved_714/Catalytic_domains/1'>two catalytic domains</scene>, linked by a proline-rich section.