3fr3: Difference between revisions

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New page: '''Unreleased structure''' The entry 3fr3 is ON HOLD Authors: Description: Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypi...
 
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'''Unreleased structure'''


The entry 3fr3 is ON HOLD
==Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118==
<StructureSection load='3fr3' size='340' side='right'caption='[[3fr3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<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'>[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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/3fr3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fr3 ConSurf].
<div style="clear:both"></div>


Authors:  
==See Also==
 
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
Description: Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118
== References ==
 
<references/>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 14 12:56:14 2009''
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Liebau E]]
[[Category: Perbandt M]]
[[Category: Ricci G]]

Latest revision as of 15:31, 1 November 2023

Tetramerization and Cooperativity in Plasmodium falciparum glutathione transferase are mediated by the atypic loop 113-118

3fr3, resolution 1.90Å

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