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2vcv
From Proteopedia
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==Glutathione transferase A3-3 in complex with glutathione and delta-4- androstene-3-17-dione== | ==Glutathione transferase A3-3 in complex with glutathione and delta-4- androstene-3-17-dione== | ||
| - | <StructureSection load='2vcv' size='340' side='right' caption='[[2vcv]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='2vcv' size='340' side='right'caption='[[2vcv]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vcv]] is a 16 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2vcv]] is a 16 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=2VCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VCV FirstGlance]. <br> |
| - | </ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr> | |
| - | <tr><td class="sblockLbl"><b> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vcv OCA], [https://pdbe.org/2vcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vcv RCSB], [https://www.ebi.ac.uk/pdbsum/2vcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vcv ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </table> |
| - | <table> | + | == Function == |
| + | [https://www.uniprot.org/uniprot/GSTA3_HUMAN GSTA3_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively.<ref>PMID:15595823</ref> <ref>PMID:20083122</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/2vcv_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vc/2vcv_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=2vcv ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases.,Tars K, Olin B, Mannervik B J Mol Biol. 2010 Mar 19;397(1):332-40. Epub 2010 Jan 18. PMID:20083122<ref>PMID:20083122</ref> | Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases.,Tars K, Olin B, Mannervik B J Mol Biol. 2010 Mar 19;397(1):332-40. Epub 2010 Jan 18. PMID:20083122<ref>PMID:20083122</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | <div class="pdbe-citations 2vcv" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mannervik B]] |
| - | [[Category: | + | [[Category: Olin B]] |
| - | [[Category: | + | [[Category: Tars K]] |
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Current revision
Glutathione transferase A3-3 in complex with glutathione and delta-4- androstene-3-17-dione
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