3rpp

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<StructureSection load='3rpp' size='340' side='right'caption='[[3rpp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3rpp' size='340' side='right'caption='[[3rpp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rpp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rpp]] is a 3 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=3RPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPP FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rpn|3rpn]]</div></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]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTK1, HDCMD47P ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3rpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpp OCA], [https://pdbe.org/3rpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpp RCSB], [https://www.ebi.ac.uk/pdbsum/3rpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpp ProSAT]</span></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=3rpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpp OCA], [https://pdbe.org/3rpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpp RCSB], [https://www.ebi.ac.uk/pdbsum/3rpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GSTK1_HUMAN GSTK1_HUMAN]] Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
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[https://www.uniprot.org/uniprot/GSTK1_HUMAN GSTK1_HUMAN] Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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GSTs (glutathione transferases) are a family of enzymes that primarily catalyse nucleophilic addition of the thiol of GSH (reduced glutathione) to a variety of hydrophobic electrophiles in the cellular detoxification of cytotoxic and genotoxic compounds. GSTks (Kappa class GSTs) are a distinct class because of their unique cellular localization, function and structure. In the present paper we report the crystal structures of hGSTk (human GSTk) in apo-form and in complex with GTX (S-hexylglutathione) and steady-state kinetic studies, revealing insights into the catalytic mechanism of hGSTk and other GSTks. Substrate binding induces a conformational change of the active site from an 'open' conformation in the apo-form to a 'closed' conformation in the GTX-bound complex, facilitating formations of the G site (GSH-binding site) and the H site (hydrophobic substrate-binding site). The conserved Ser(16) at the G site functions as the catalytic residue in the deprotonation of the thiol group and the conserved Asp(69), Ser(200), Asp(201) and Arg(202) form a network of interactions with gamma-glutamyl carboxylate to stabilize the thiolate anion. The H site is a large hydrophobic pocket with conformational flexibility to allow the binding of different hydrophobic substrates. The kinetic mechanism of hGSTk conforms to a rapid equilibrium random sequential Bi Bi model.
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Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism.,Wang B, Peng Y, Zhang T, Ding J Biochem J. 2011 Oct 15;439(2):215-25. PMID:21728995<ref>PMID:21728995</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rpp" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glutathione transferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ding, J]]
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[[Category: Ding J]]
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[[Category: Peng, Y]]
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[[Category: Peng Y]]
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[[Category: Wang, B]]
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[[Category: Wang B]]
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[[Category: Zhang, T]]
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[[Category: Zhang T]]
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[[Category: Apo form]]
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[[Category: Detoxification]]
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[[Category: Gsh binding]]
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[[Category: Kappa gst]]
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[[Category: Transferase]]
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[[Category: Trx domain]]
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Current revision

Crystal structure of human kappa class glutathione transferase in apo form

PDB ID 3rpp

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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