3l0h

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[[Image:3l0h.png|left|200px]]
 
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{{STRUCTURE_3l0h| PDB=3l0h | SCENE= }}
{{STRUCTURE_3l0h| PDB=3l0h | SCENE= }}
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===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===
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{{ABSTRACT_PUBMED_20833278}}
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==Function==
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[[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>
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{{ABSTRACT_PUBMED_20833278}}
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==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].
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==See Also==
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*[[Glutathione S-transferase|Glutathione S-transferase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:20833278</ref><references group="xtra"/>
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<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.]]
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[[Category: Glutathione s-transferase]]
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[[Category: S-hexylglutathione]]
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[[Category: Thioredoxin]]
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[[Category: Transferase]]

Revision as of 20:23, 4 April 2013

Template:STRUCTURE 3l0h

Contents

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
  1. 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

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