6ato

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:24, 4 October 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6ato' size='340' side='right'caption='[[6ato]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
<StructureSection load='6ato' size='340' side='right'caption='[[6ato]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6ato]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ATO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ATO FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6ato]] 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=6ATO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ATO FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <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]] 1.55&#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=GSH:GLUTATHIONE'>GSH</scene>, <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=6ato FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ato OCA], [http://pdbe.org/6ato PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ato RCSB], [http://www.ebi.ac.uk/pdbsum/6ato PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ato 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=6ato FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ato OCA], [https://pdbe.org/6ato PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ato RCSB], [https://www.ebi.ac.uk/pdbsum/6ato PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ato ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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 6ato" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 26: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Glutathione transferase]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Ji, X]]
+
[[Category: Ji X]]
-
[[Category: Kumari, V]]
+
[[Category: Kumari V]]
-
[[Category: Glutathione s-transferase]]
+
-
[[Category: Gsh]]
+
-
[[Category: Gst]]
+
-
[[Category: Hgsta1-1]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of hGSTA1-1 complexed with GSH and MPD in each subunit

PDB ID 6ato

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6ato"
Personal tools