Sandbox Reserved 714

(Difference between revisions)

Revision as of 19:45, 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

DUTREUX Fabien, BONHOURE Anna

@@ Line 15: / Line 15: @@
 The Human soluble Epoxide hydrolase is a homodimer. Each subunit has <scene name='Sandbox_Reserved_714/Catalytic_domains/3'>two catalytic domains</scene>, linked by a proline-rich section.
-The C-terminal domain is called Cytosolic epoxide hydrolase 2: it catalyzes the trans-addition of water to epoxides in order to product glycols. The <scene name='Sandbox_Reserved_714/Cter_activesite/3'>active site</scene> is made of five residues. The 3D structure of this active site is maintained by hydrogen bonds, including those created by D496. The two tyrosines (Y383 and Y466) assist the proper positioning of the substrate by polarizing it, thanks to their hydroxyl groups. D335 plays the role of the nucleophilic acid. Finally, H524 plays the role of a base in order to release the final product.
 == Mechanism ==
+The C-terminal domain is called Cytosolic epoxide hydrolase 2: it catalyzes the trans-addition of water to epoxides in order to product glycols. The <scene name='Sandbox_Reserved_714/Cter_activesite/3'>active site</scene> is made of five residues. The 3D structure of this active site is maintained by hydrogen bonds, including those created by D496. The two tyrosines (Y383 and Y466) assist the proper positioning of the substrate by polarizing it, thanks to their hydroxyl groups. D335 plays the role of the nucleophilic acid. Finally, H524 plays the role of a base in order to release the final product.