1cr6: Difference between revisions

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{{Seed}}
[[Image:1cr6.png|left|200px]]


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==CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR==
The line below this paragraph, containing "STRUCTURE_1cr6", creates the "Structure Box" on the page.
<StructureSection load='1cr6' size='340' side='right'caption='[[1cr6]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1cr6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CR6 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPU:N-CYCLOHEXYL-N-(PROPYL)PHENYL+UREA'>CPU</scene></td></tr>
{{STRUCTURE_1cr6| PDB=1cr6 |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cr6 OCA], [https://pdbe.org/1cr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cr6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HYES_MOUSE HYES_MOUSE] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cr/1cr6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cr6 ConSurf].
<div style="clear:both"></div>


===CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR===
==See Also==
 
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
 
__TOC__
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</StructureSection>
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[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10485878 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10485878}}
 
==About this Structure==
1CR6 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CR6 OCA].
 
==Reference==
<ref group="xtra">PMID:10485878</ref><references group="xtra"/>
[[Category: Microsomal epoxide hydrolase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Argiriadi, M A.]]
[[Category: Argiriadi MA]]
[[Category: Christianson, D W.]]
[[Category: Christianson DW]]
[[Category: Hammock, B D.]]
[[Category: Hammock BD]]
[[Category: Morisseau, C.]]
[[Category: Morisseau C]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Disubstituted urea inhibitor]]
[[Category: Homodimer]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:46:58 2009''

Latest revision as of 09:45, 7 February 2024

CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITORCRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR

Structural highlights

1cr6 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HYES_MOUSE Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1cr6, resolution 2.80Å

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