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3fr3
From Proteopedia
(Difference between revisions)
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<StructureSection load='3fr3' size='340' side='right'caption='[[3fr3]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3fr3' size='340' side='right'caption='[[3fr3]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3fr3]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3fr3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FR3 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=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fr3 OCA], [https://pdbe.org/3fr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fr3 RCSB], [https://www.ebi.ac.uk/pdbsum/3fr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fr3 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/GST_PLAF7 GST_PLAF7] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May also function as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin IX (hemin).<ref>PMID:12108547</ref> <ref>PMID:12387854</ref> <ref>PMID:16385005</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> | ||
| - | [[Category: Glutathione transferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Plafa]] | ||
| - | [[Category: Liebau, E]] | ||
| - | [[Category: Perbandt, M]] | ||
| - | [[Category: Ricci, G]] | ||
| - | [[Category: Oxidative stress]] | ||
| - | [[Category: Pfgst]] | ||
[[Category: Plasmodium falciparum]] | [[Category: Plasmodium falciparum]] | ||
| - | [[Category: | + | [[Category: Liebau E]] |
| + | [[Category: Perbandt M]] | ||
| + | [[Category: Ricci G]] | ||
Current revision
Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
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