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1px6

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==A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine==
==A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine==
<StructureSection load='1px6' size='340' side='right' caption='[[1px6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1px6' size='340' side='right' caption='[[1px6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1px7|1px7]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1px7|1px7]]</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>
<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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<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=1px6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px6 OCA], [http://pdbe.org/1px6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1px6 RCSB], [http://www.ebi.ac.uk/pdbsum/1px6 PDBsum]</span></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=1px6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px6 OCA], [http://pdbe.org/1px6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1px6 RCSB], [http://www.ebi.ac.uk/pdbsum/1px6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1px6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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=1px6 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=1px6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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==See Also==
 
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*[[Glutathione S-transferase|Glutathione S-transferase]]
 
== References ==
== References ==
<references/>
<references/>

Revision as of 09:50, 12 October 2017

A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine

1px6, resolution 2.10Å

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