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1px7

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Current revision (07:22, 25 October 2023) (edit) (undo)
 
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<StructureSection load='1px7' size='340' side='right'caption='[[1px7]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
<StructureSection load='1px7' size='340' side='right'caption='[[1px7]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1px7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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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<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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</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>
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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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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1px6|1px6]]</div></td></tr>
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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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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
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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>
<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>
</table>
== Function ==
== Function ==
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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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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutathione transferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[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: Helix capping]]
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[[Category: Mutation]]
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[[Category: Protein folding]]
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[[Category: Transferase]]
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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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