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[[Image:2aaq.gif|left|200px]]


{{Structure
==Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI==
|PDB= 2aaq |SIZE=350|CAPTION= <scene name='initialview01'>2aaq</scene>, resolution 2.60&Aring;
<StructureSection load='2aaq' size='340' side='right'caption='[[2aaq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=AUP:2-(2-PHENYL-3-PYRIDIN-2-YL-4,5,6,7-TETRAHYDRO-2H-ISOPHOSPHINDOL-1-YL)PYRIDINE'>AUP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
<table><tr><td colspan='2'>[[2aaq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AAQ FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
|GENE= hGR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene>, <scene name='pdbligand=AUP:2-(2-PHENYL-3-PYRIDIN-2-YL-4,5,6,7-TETRAHYDRO-2H-ISOPHOSPHINDOL-1-YL)PYRIDINE'>AUP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaq OCA], [https://pdbe.org/2aaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aaq RCSB], [https://www.ebi.ac.uk/pdbsum/2aaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aaq ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaq OCA], [http://www.ebi.ac.uk/pdbsum/2aaq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aaq RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN] Maintains high levels of reduced glutathione in the cytosol.
== 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/aa/2aaq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2aaq ConSurf].
<div style="clear:both"></div>


'''Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI'''
==See Also==
 
*[[Glutathione Reductase|Glutathione Reductase]]
 
__TOC__
==About this Structure==
</StructureSection>
2AAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAQ OCA].
 
==Reference==
Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases., Urig S, Fritz-Wolf K, Reau R, Herold-Mende C, Toth K, Davioud-Charvet E, Becker K, Angew Chem Int Ed Engl. 2006 Mar 13;45(12):1881-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16493712 16493712]
[[Category: Glutathione-disulfide reductase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Becker, K.]]
[[Category: Becker K]]
[[Category: Davioud-Charvet, E.]]
[[Category: Davioud-Charvet E]]
[[Category: Fritz-Wolf, K.]]
[[Category: Fritz-Wolf K]]
[[Category: Herold-Mende, C.]]
[[Category: Herold-Mende C]]
[[Category: Reau, R.]]
[[Category: Reau R]]
[[Category: Toth, K.]]
[[Category: Toth K]]
[[Category: Urig, S.]]
[[Category: Urig S]]
[[Category: antioxidative system]]
[[Category: disulfide reductase]]
[[Category: glutathione reduction]]
[[Category: gold-coordination]]
[[Category: homodimer]]
[[Category: protein gold complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:50:15 2008''
Retrieved from "https://proteopedia.org/2aaq"