1ehy
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ehy |SIZE=350|CAPTION= <scene name='initialview01'>1ehy</scene>, resolution 2.1Å | |PDB= 1ehy |SIZE=350|CAPTION= <scene name='initialview01'>1ehy</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=K:POTASSIUM ION'>K</scene> | + | |LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Microsomal_epoxide_hydrolase Microsomal epoxide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 3.3.2.9] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Microsomal_epoxide_hydrolase Microsomal epoxide hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.9 3.3.2.9] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ehy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehy OCA], [http://www.ebi.ac.uk/pdbsum/1ehy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ehy RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Rink, R.]] | [[Category: Rink, R.]] | ||
[[Category: Rozeboom, H J.]] | [[Category: Rozeboom, H J.]] | ||
| - | [[Category: K]] | ||
[[Category: alpha/beta hydrolase fold]] | [[Category: alpha/beta hydrolase fold]] | ||
[[Category: epichlorohydrin]] | [[Category: epichlorohydrin]] | ||
| Line 36: | Line 38: | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:02:54 2008'' |
Revision as of 17:02, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Microsomal epoxide hydrolase, with EC number 3.3.2.9 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray structure of the epoxide hydrolase from agrobacterium radiobacter ad1
Overview
Epoxide hydrolases catalyze the cofactor-independent hydrolysis of reactive and toxic epoxides. They play an essential role in the detoxification of various xenobiotics in higher organisms and in the bacterial degradation of several environmental pollutants. The first x-ray structure of one of these, from Agrobacterium radiobacter AD1, has been determined by isomorphous replacement at 2.1-A resolution. The enzyme shows a two-domain structure with the core having the alpha/beta hydrolase-fold topology. The catalytic residues, Asp107 and His275, are located in a predominantly hydrophobic environment between the two domains. A tunnel connects the back of the active-site cavity with the surface of the enzyme and provides access to the active site for the catalytic water molecule, which in the crystal structure, has been found at hydrogen bond distance to His275. Because of a crystallographic contact, the active site has become accessible for the Gln134 side chain, which occupies a position mimicking a bound substrate. The structure suggests Tyr152/Tyr215 as the residues involved in substrate binding, stabilization of the transition state, and possibly protonation of the epoxide oxygen.
About this Structure
1EHY is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.
Reference
The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides., Nardini M, Ridder IS, Rozeboom HJ, Kalk KH, Rink R, Janssen DB, Dijkstra BW, J Biol Chem. 1999 May 21;274(21):14579-86. PMID:10329649
Page seeded by OCA on Sun Mar 30 20:02:54 2008
