3l0h: Difference between revisions
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{{STRUCTURE_3l0h| PDB=3l0h | SCENE= }} | {{STRUCTURE_3l0h| PDB=3l0h | SCENE= }} | ||
===Crystal Structure Analysis of W21A mutant of human GSTA1-1 in complex with S-hexylglutathione=== | ===Crystal Structure Analysis of W21A mutant of human GSTA1-1 in complex with S-hexylglutathione=== | ||
{{ABSTRACT_PUBMED_20833278}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[3l0h]] 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=3L0H OCA]. | [[3l0h]] 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=3L0H OCA]. | ||
==See Also== | |||
*[[Glutathione S-transferase|Glutathione S-transferase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:020833278</ref><references group="xtra"/><references/> | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Fanucchi, S.]] | [[Category: Fanucchi, S.]] | ||
[[Category: Fernandes, M A.]] | [[Category: Fernandes, M A.]] | ||
[[Category: Glutathione s-transferase]] | |||
[[Category: S-hexylglutathione]] | |||
[[Category: Thioredoxin]] | |||
[[Category: Transferase]] | |||
Revision as of 20:23, 4 April 2013
Crystal Structure Analysis of W21A mutant of human GSTA1-1 in complex with S-hexylglutathione
Template:ABSTRACT PUBMED 20833278
Function
[GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.[1]
About this Structure
3l0h is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Balchin D, Fanucchi S, Achilonu I, Adamson RJ, Burke J, Fernandes M, Gildenhuys S, Dirr HW. Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1. Biochim Biophys Acta. 2010 Sep 15. PMID:20833278 doi:10.1016/j.bbapap.2010.09.003
- ↑ Achilonu I, Gildenhuys S, Fisher L, Burke J, Fanucchi S, Sewell BT, Fernandes M, Dirr HW. The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jul 1;66(Pt, 7):776-80. Epub 2010 Jun 23. PMID:20606271 doi:10.1107/S1744309110019135