1cr6: Difference between revisions
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|PDB= 1cr6 |SIZE=350|CAPTION= <scene name='initialview01'>1cr6</scene>, resolution 2.8Å | |PDB= 1cr6 |SIZE=350|CAPTION= <scene name='initialview01'>1cr6</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CPU:N-CYCLOHEXYL-N'-(PROPYL)PHENYL UREA'>CPU</scene> | |LIGAND= <scene name='pdbligand=CPU:N-CYCLOHEXYL-N'-(PROPYL)PHENYL+UREA'>CPU</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=[[1cqz|1CQZ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cr6 OCA], [http://www.ebi.ac.uk/pdbsum/1cr6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cr6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Hammock, B D.]] | [[Category: Hammock, B D.]] | ||
[[Category: Morisseau, C.]] | [[Category: Morisseau, C.]] | ||
[[Category: alpha/beta hydrolase fold]] | [[Category: alpha/beta hydrolase fold]] | ||
[[Category: disubstituted urea inhibitor]] | [[Category: disubstituted urea inhibitor]] | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:27:00 2008'' | ||
Revision as of 19:27, 30 March 2008
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| , resolution 2.8Å | |||||||
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| Ligands: | |||||||
| Activity: | Microsomal epoxide hydrolase, with EC number 3.3.2.9 | ||||||
| Related: | 1CQZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR
OverviewOverview
The crystal structure of recombinant murine liver cytosolic epoxide hydrolase (EC 3.3.2.3) has been determined at 2.8-A resolution. The binding of a nanomolar affinity inhibitor confirms the active site location in the C-terminal domain; this domain is similar to that of haloalkane dehalogenase and shares the alpha/beta hydrolase fold. A structure-based mechanism is proposed that illuminates the unique chemical strategy for the activation of endogenous and man-made epoxide substrates for hydrolysis and detoxification. Surprisingly, a vestigial active site is found in the N-terminal domain similar to that of another enzyme of halocarbon metabolism, haloacid dehalogenase. Although the vestigial active site does not participate in epoxide hydrolysis, the vestigial domain plays a critical structural role by stabilizing the dimer in a distinctive domain-swapped architecture. Given the genetic and structural relationships among these enzymes of xenobiotic metabolism, a structure-based evolutionary sequence is postulated.
About this StructureAbout this Structure
1CR6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase., Argiriadi MA, Morisseau C, Hammock BD, Christianson DW, Proc Natl Acad Sci U S A. 1999 Sep 14;96(19):10637-42. PMID:10485878
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