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5dal

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==Crystal Structure of human Glutathione Transferase Pi complexed with a metalloid in the presence of Glutathione==
==Crystal Structure of human Glutathione Transferase Pi complexed with a metalloid in the presence of Glutathione==
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<StructureSection load='5dal' size='340' side='right' caption='[[5dal]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='5dal' size='340' side='right'caption='[[5dal]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dal]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DAL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DAL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dal]] 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=5DAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DAL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5AU:DI-GLUTATHIONE-PHENYLARSINE'>5AU</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PA0:PHENYLARSINE+OXIDE'>PA0</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=5AU:DI-GLUTATHIONE-PHENYLARSINE'>5AU</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PA0:PHENYLARSINE+OXIDE'>PA0</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dak|5dak]], [[5dcg|5dcg]], [[5ddl|5ddl]]</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=5dal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dal OCA], [https://pdbe.org/5dal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dal RCSB], [https://www.ebi.ac.uk/pdbsum/5dal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dal ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dal OCA], [http://pdbe.org/5dal PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dal RCSB], [http://www.ebi.ac.uk/pdbsum/5dal PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dal ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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>
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutathione transferase]]
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[[Category: Homo sapiens]]
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[[Category: Morton, C J]]
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[[Category: Large Structures]]
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[[Category: Parker, L J]]
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[[Category: Morton CJ]]
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[[Category: Parker, M W]]
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[[Category: Parker LJ]]
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[[Category: Anti-cancer]]
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[[Category: Parker MW]]
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[[Category: Metalloid]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of human Glutathione Transferase Pi complexed with a metalloid in the presence of Glutathione

PDB ID 5dal

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