5djm
From Proteopedia
(Difference between revisions)
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<StructureSection load='5djm' size='340' side='right'caption='[[5djm]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5djm' size='340' side='right'caption='[[5djm]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5djm]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5djm]] 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=5DJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DJM FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5djm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djm OCA], [https://pdbe.org/5djm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5djm RCSB], [https://www.ebi.ac.uk/pdbsum/5djm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5djm ProSAT]</span></td></tr> |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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> |
==See Also== | ==See Also== | ||
| - | *[[Glutathione S-transferase|Glutathione S-transferase]] | + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Parker | + | [[Category: Parker LJ]] |
| - | + | ||
| - | + | ||
Current revision
Structure of WT Human Glutathione Transferase in complex with cisplatin in the absence of glutathione.
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