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1guh

From Proteopedia

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[[Image:1guh.gif|left|200px]]
 
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{{Structure
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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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|PDB= 1guh |SIZE=350|CAPTION= <scene name='initialview01'>1guh</scene>, resolution 2.6&Aring;
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<StructureSection load='1guh' size='340' side='right'caption='[[1guh]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GSB:S-BENZYL-GLUTATHIONE'>GSB</scene>
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1guh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1guh OCA], [http://www.ebi.ac.uk/pdbsum/1guh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1guh RCSB]</span>
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== Function ==
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}}
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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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'''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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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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1GUH 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=1GUH OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/8331657 8331657]
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[[Category: Glutathione transferase]]
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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: 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: transferase(glutathione)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:33 2008''
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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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