3f6d

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{{STRUCTURE_3f6d| PDB=3f6d | SCENE= }}
{{STRUCTURE_3f6d| PDB=3f6d | SCENE= }}
===Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles dirus, F123A, in Complex with S-Hexyl Glutathione===
===Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles dirus, F123A, in Complex with S-Hexyl Glutathione===
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{{ABSTRACT_PUBMED_20196771}}
{{ABSTRACT_PUBMED_20196771}}
==About this Structure==
==About this Structure==
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3F6D is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F6D OCA].
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[[3f6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F6D 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:20196771</ref><references group="xtra"/>
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<ref group="xtra">PMID:020196771</ref><references group="xtra"/>
[[Category: Anopheles dirus]]
[[Category: Anopheles dirus]]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
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[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:27:18 2010''
 

Revision as of 11:07, 13 February 2013

Template:STRUCTURE 3f6d

Contents

Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles dirus, F123A, in Complex with S-Hexyl Glutathione

Template:ABSTRACT PUBMED 20196771

About this Structure

3f6d is a 2 chain structure with sequence from Anopheles dirus. Full crystallographic information is available from OCA.

See Also

Reference

  • Wongsantichon J, Robinson RC, Ketterman AJ. Structural contributions of delta class glutathione transferase active-site residues to catalysis. Biochem J. 2010 Apr 28;428(1):25-32. PMID:20196771 doi:10.1042/BJ20091939

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