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Sandbox Reserved 714

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== Overview ==
== Overview ==
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== Structure ==
 
<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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== Structure ==
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.
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.
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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/1'>active site</scene> is made of five residues. The two tyrosines (Y383 and Y466) plays a role.

Revision as of 19:10, 30 December 2012

PDB ID 1s8o

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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
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Human Soluble Epoxide Hydrolase: Biological assembly, 1s8o
Human Soluble Epoxide Hydrolase: Biological assembly, 1s8o

Contents

Overview

X-ray crystal structure of hsEH

Drag the structure with the mouse to rotate

Structure

The Human soluble Epoxide hydrolase is a homodimer. Each subunit has , 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 is made of five residues. The two tyrosines (Y383 and Y466) plays a role.


Mechanism

Inhibitors

External ressources

References

Proteopedia Page Contributors and Editors

DUTREUX Fabien, BONHOURE Anna

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