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1px6
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1px6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PX6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1px6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PX6 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> |
| - | <tr><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><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> |
| - | <tr><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://www.rcsb.org/pdb/explore.do?structureId=1px6 RCSB], [http://www.ebi.ac.uk/pdbsum/1px6 PDBsum]</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=1px6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1px6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1px6 RCSB], [http://www.ebi.ac.uk/pdbsum/1px6 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Glutathione S-transferase|Glutathione S-transferase]] | *[[Glutathione S-transferase|Glutathione S-transferase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Aceto, A | + | [[Category: Aceto, A]] |
| - | [[Category: Dragani, B | + | [[Category: Dragani, B]] |
| - | [[Category: Kong, G K.W | + | [[Category: Kong, G K.W]] |
| - | [[Category: Mannervik, B | + | [[Category: Mannervik, B]] |
| - | [[Category: McKinstry, W J | + | [[Category: McKinstry, W J]] |
| - | [[Category: Paludi, D | + | [[Category: Paludi, D]] |
| - | [[Category: Parker, M W | + | [[Category: Parker, M W]] |
| - | [[Category: Polekhina, G | + | [[Category: Polekhina, G]] |
| - | [[Category: Principe, D R | + | [[Category: Principe, D R]] |
| - | [[Category: Stenberg, G | + | [[Category: Stenberg, G]] |
| - | + | ||
[[Category: Helix capping]] | [[Category: Helix capping]] | ||
[[Category: Mutation]] | [[Category: Mutation]] | ||
[[Category: Protein folding]] | [[Category: Protein folding]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 11:34, 25 December 2014
A folding mutant of human class pi glutathione transferase, created by mutating aspartate 153 of the wild-type protein to asparagine
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