1y6e

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<StructureSection load='1y6e' size='340' side='right'caption='[[1y6e]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1y6e' size='340' side='right'caption='[[1y6e]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1y6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y6E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1y6e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_japonicum Schistosoma japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y6E FirstGlance]. <br>
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</td></tr><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>
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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]] 3&#8491;</td></tr>
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<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=1y6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y6e OCA], [http://pdbe.org/1y6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y6e RCSB], [http://www.ebi.ac.uk/pdbsum/1y6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y6e ProSAT]</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=1y6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y6e OCA], [https://pdbe.org/1y6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y6e RCSB], [https://www.ebi.ac.uk/pdbsum/1y6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y6e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1y6e ConSurf].
</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=1y6e ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of the 26 kDa glutathione S-transferase from Schistosoma japonicum (SjGST) was determined at 3 A resolution in the new space group P2(1)2(1)2(1). The structure of orthorhombic SjGST reveals unique features of the ligand-binding site and dimer interface when compared with previously reported structures. SjGST is recognized as the major detoxification enzyme of S. japonicum, a pathogenic helminth causing schistosomiasis. As resistance against the established inhibitor of SjGST, praziquantel, has been reported these results might prove to be valuable for the development of novel drugs.
 
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X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site.,Rufer AC, Thiebach L, Baer K, Klein HW, Hennig M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt, 3):263-5. Epub 2005 Feb 24. PMID:16511012<ref>PMID:16511012</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 1y6e" style="background-color:#fffaf0;"></div>
 
==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: Blood fluke]]
 
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[[Category: Glutathione transferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baer, K]]
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[[Category: Schistosoma japonicum]]
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[[Category: Hennig, M]]
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[[Category: Baer K]]
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[[Category: Klein, H W]]
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[[Category: Hennig M]]
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[[Category: Rufer, A C]]
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[[Category: Klein HW]]
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[[Category: Thiebach, L]]
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[[Category: Rufer AC]]
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[[Category: Dimer]]
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[[Category: Thiebach L]]
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[[Category: Transferase]]
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Current revision

Orthorhombic glutathione S-transferase of Schistosoma japonicum

PDB ID 1y6e

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