3lfl
From Proteopedia
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m (Protected "3lfl" [edit=sysop:move=sysop]) |
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021106529</ref><references group="xtra"/> |
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: J., Brock.]] | [[Category: J., Brock.]] | ||
| + | [[Category: C-terminal alpha-helical domain]] | ||
| + | [[Category: Glutathione s-transferase omega 1 del155]] | ||
| + | [[Category: N-terminal thioredoxin-like domain]] | ||
| + | [[Category: Protein-glutathione complex]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:34, 14 December 2011
Crystal Structure of human Glutathione Transferase Omega 1, delta 155
Template:ABSTRACT PUBMED 21106529
About this Structure
3lfl is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Zhou H, Brock J, Casarotto MG, Oakley AJ, Board PG. Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1. J Biol Chem. 2011 Feb 11;286(6):4271-9. Epub 2010 Nov 24. PMID:21106529 doi:10.1074/jbc.M110.197822
