2aaq

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(New page: 200px<br /> <applet load="2aaq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aaq, resolution 2.60&Aring;" /> '''Crystal Structure A...)
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[[Image:2aaq.gif|left|200px]]<br />
 
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<applet load="2aaq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2aaq, resolution 2.60&Aring;" />
 
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'''Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI'''<br />
 
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==Disease==
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==Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI==
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Known disease associated with this structure: Hemolytic anemia due to glutathione reductase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138300 138300]]
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<StructureSection load='2aaq' size='340' side='right'caption='[[2aaq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN] Maintains high levels of reduced glutathione in the cytosol.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/2aaq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2AAQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4, CL, K, FAD, AUP, AU and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AAQ OCA].
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*[[Glutathione Reductase|Glutathione Reductase]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16493712 16493712]
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[[Category: Glutathione-disulfide reductase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Becker, K.]]
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[[Category: Becker K]]
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[[Category: Davioud-Charvet, E.]]
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[[Category: Davioud-Charvet E]]
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[[Category: Fritz-Wolf, K.]]
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[[Category: Fritz-Wolf K]]
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[[Category: Herold-Mende, C.]]
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[[Category: Herold-Mende C]]
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[[Category: Reau, R.]]
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[[Category: Reau R]]
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[[Category: Toth, K.]]
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[[Category: Toth K]]
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[[Category: Urig, S.]]
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[[Category: Urig S]]
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[[Category: AU]]
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[[Category: AUP]]
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[[Category: CL]]
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[[Category: FAD]]
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[[Category: GOL]]
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[[Category: K]]
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[[Category: PO4]]
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[[Category: antioxidative system]]
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[[Category: disulfide reductase]]
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[[Category: glutathione reduction]]
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[[Category: gold-coordination]]
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[[Category: homodimer]]
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[[Category: protein gold complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:48:06 2007''
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Current revision

Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI

PDB ID 2aaq

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