6ji6
From Proteopedia
(Difference between revisions)
m (Protected "6ji6" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of glutathione S-transferase complexed and modified with glutathione== | |
| - | + | <StructureSection load='6ji6' size='340' side='right'caption='[[6ji6]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ji6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JI6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JI6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | |
| - | [[Category: | + | <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> |
| + | <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=6ji6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ji6 OCA], [http://pdbe.org/6ji6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ji6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ji6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ji6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GST26_SCHJA GST26_SCHJA]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glutathione transferase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Arai, R]] | [[Category: Arai, R]] | ||
[[Category: Okajima, T]] | [[Category: Okajima, T]] | ||
| + | [[Category: Glutathione s-transferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 08:01, 20 March 2019
Crystal structure of glutathione S-transferase complexed and modified with glutathione
| |||||||||||
