6atp: Difference between revisions

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 <StructureSection load='6atp' size='340' side='right'caption='[[6atp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6atp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ATP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ATP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6atp]] is a 2 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=6ATP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ATP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6atp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6atp OCA], [http://pdbe.org/6atp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6atp RCSB], [http://www.ebi.ac.uk/pdbsum/6atp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6atp ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6atp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6atp OCA], [https://pdbe.org/6atp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6atp RCSB], [https://www.ebi.ac.uk/pdbsum/6atp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6atp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:8331657<ref>PMID:8331657</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6atp" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Glutathione transferase]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Ji, X]]
+[[Category: Ji X]]
-[[Category: Kumari, V]]
+[[Category: Kumari V]]
-[[Category: Apo]]
-[[Category: Glutathione s-transferase]]
-[[Category: Gst]]
-[[Category: Hgsta1-1]]
-[[Category: Transferase]]