1px7: Difference between revisions

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New page: left|200px<br /> <applet load="1px7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1px7, resolution 2.03Å" /> '''A folding mutant of...
 
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[[Image:1px7.gif|left|200px]]<br />
<applet load="1px7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1px7, resolution 2.03&Aring;" />
'''A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate'''<br />


==About this Structure==
==A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate==
1PX7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, MES and GSH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PX7 OCA].  
<StructureSection load='1px7' size='340' side='right'caption='[[1px7]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
[[Category: Glutathione transferase]]
== 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]] 2.03&#8491;</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: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aceto, A.]]
[[Category: Aceto A]]
[[Category: Dragani, B.]]
[[Category: Dragani B]]
[[Category: Kong, G.K.W.]]
[[Category: Kong GK-W]]
[[Category: Mannervik, B.]]
[[Category: Mannervik B]]
[[Category: McKinstry, W.J.]]
[[Category: McKinstry WJ]]
[[Category: Paludi, D.]]
[[Category: Paludi D]]
[[Category: Parker, M.W.]]
[[Category: Parker MW]]
[[Category: Polekhina, G.]]
[[Category: Polekhina G]]
[[Category: Principe, D.R.]]
[[Category: Principe DR]]
[[Category: Stenberg, G.]]
[[Category: Stenberg G]]
[[Category: CA]]
[[Category: GSH]]
[[Category: MES]]
[[Category: glutathione transferase]]
[[Category: helix capping]]
[[Category: mutations]]
[[Category: protein folding]]
[[Category: x-ray crystallography]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:47:59 2007''

Latest revision as of 07:22, 25 October 2023

A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to glutamate

1px7, resolution 2.03Å

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