1px7
From Proteopedia
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- | [[Image:1px7.jpg|left|200px]]<br /><applet load="1px7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
- | caption="1px7, resolution 2.03Å" /> | ||
- | '''A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate'''<br /> | ||
- | == | + | ==A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate== |
- | + | <StructureSection load='1px7' size='340' side='right'caption='[[1px7]], [[Resolution|resolution]] 2.03Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1px7]] 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=1PX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PX7 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]] 2.03Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=1px7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px7 OCA], [https://pdbe.org/1px7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1px7 RCSB], [https://www.ebi.ac.uk/pdbsum/1px7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1px7 ProSAT]</span></td></tr> |
- | [ | + | </table> |
- | + | == Function == | |
- | + | [https://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref> | |
- | [ | + | == Evolutionary Conservation == |
- | [ | + | [[Image:Consurf_key_small.gif|200px|right]] |
- | [[ | + | Check<jmol> |
- | + | <jmolCheckbox> | |
- | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/px/1px7_consurf.spt"</scriptWhenChecked> | |
- | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
- | + | <text>to colour the structure by Evolutionary Conservation</text> | |
- | [ | + | </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/main_output.php?pdb_ID=1px7 ConSurf]. |
- | [ | + | <div style="clear:both"></div> |
- | + | ||
- | + | ||
- | + | ||
- | + | ==See Also== | |
+ | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Aceto A]] | ||
+ | [[Category: Dragani B]] | ||
+ | [[Category: Kong GK-W]] | ||
+ | [[Category: Mannervik B]] | ||
+ | [[Category: McKinstry WJ]] | ||
+ | [[Category: Paludi D]] | ||
+ | [[Category: Parker MW]] | ||
+ | [[Category: Polekhina G]] | ||
+ | [[Category: Principe DR]] | ||
+ | [[Category: Stenberg G]] |
Current revision
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate
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Categories: Homo sapiens | Large Structures | Aceto A | Dragani B | Kong GK-W | Mannervik B | McKinstry WJ | Paludi D | Parker MW | Polekhina G | Principe DR | Stenberg G