1guh

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(New page: 200px<br /> <applet load="1guh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1guh, resolution 2.6&Aring;" /> '''STRUCTURE DETERMINAT...)
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[[Image:1guh.gif|left|200px]]<br />
 
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<applet load="1guh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1guh, resolution 2.6&Aring;" />
 
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'''STRUCTURE DETERMINATION AND REFINEMENT OF HUMAN ALPHA CLASS GLUTATHIONE TRANSFERASE A1-1, AND A COMPARISON WITH THE MU AND PI CLASS ENZYMES'''<br />
 
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==Overview==
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==Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes==
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The crystal structure of human alpha class glutathione transferase A1-1, has been determined and refined to a resolution of 2.6 A. There are two, copies of the dimeric enzyme in the asymmetric unit. Each monomer is built, from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily, associated with one of these domains via a network of hydrogen bonds and, salt-links. In particular, the sulphur atom of the inhibitor forms a, hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of, Arg15. The benzyl group of the inhibitor is completely buried in a, hydrophobic pocket. The structure shows an overall similarity to the mu, and pi class enzymes particularly in the glutathione-binding domain". The, main difference concerns the extended C terminus of the alpha class enzyme, which forms an extra alpha-helix that blocks one entrance to the active, site and makes up part of the substrate binding site.
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<StructureSection load='1guh' size='340' side='right'caption='[[1guh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1guh]] is a 4 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=1GUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GUH 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=GSB:S-BENZYL-GLUTATHIONE'>GSB</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=1guh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1guh OCA], [https://pdbe.org/1guh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1guh RCSB], [https://www.ebi.ac.uk/pdbsum/1guh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1guh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
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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/gu/1guh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1guh 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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1GUH 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 GSB as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUH OCA].
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes., Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG, et al., J Mol Biol. 1993 Jul 5;232(1):192-212. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8331657 8331657]
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__TOC__
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[[Category: Glutathione transferase]]
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</StructureSection>
[[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: Jones, T.A.]]
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[[Category: Jones TA]]
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[[Category: Kleywegt, G.J.]]
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[[Category: Kleywegt GJ]]
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[[Category: Sinning, I.]]
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[[Category: Sinning I]]
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[[Category: GSB]]
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[[Category: transferase(glutathione)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:09:10 2007''
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Current revision

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the MU and PI class enzymes

PDB ID 1guh

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