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1px7

From Proteopedia

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[[Image:1px7.jpg|left|200px]]
 
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{{Structure
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==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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|PDB= 1px7 |SIZE=350|CAPTION= <scene name='initialview01'>1px7</scene>, resolution 2.03&Aring;
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<StructureSection load='1px7' size='340' side='right'caption='[[1px7]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>
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<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>
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|ACTIVITY= <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>
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</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>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[1px6|1PX6]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1px7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px7 OCA], [http://www.ebi.ac.uk/pdbsum/1px7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1px7 RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/px/1px7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''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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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1PX7 is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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[[Category: Glutathione transferase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aceto, A.]]
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[[Category: Aceto A]]
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[[Category: Dragani, B.]]
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[[Category: Dragani B]]
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[[Category: Kong, G K.W.]]
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[[Category: Kong GK-W]]
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[[Category: Mannervik, B.]]
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[[Category: Mannervik B]]
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[[Category: McKinstry, W J.]]
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[[Category: McKinstry WJ]]
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[[Category: Paludi, D.]]
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[[Category: Paludi D]]
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[[Category: Parker, M W.]]
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[[Category: Parker MW]]
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[[Category: Polekhina, G.]]
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[[Category: Polekhina G]]
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[[Category: Principe, D R.]]
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[[Category: Principe DR]]
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[[Category: Stenberg, G.]]
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[[Category: Stenberg G]]
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[[Category: glutathione transferase]]
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[[Category: helix capping]]
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[[Category: mutation]]
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[[Category: protein folding]]
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[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:05:45 2008''
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Current revision

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

PDB ID 1px7

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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