3f6d: Difference between revisions
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[[Image:3f6d.png|left|200px]] | [[Image:3f6d.png|left|200px]] | ||
{{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=== | ||
{{ABSTRACT_PUBMED_20196771}} | {{ABSTRACT_PUBMED_20196771}} | ||
==About this Structure== | ==About this Structure== | ||
[[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]. | |||
==See Also== | |||
*[[Glutathione S-transferase|Glutathione S-transferase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <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]] | ||
Revision as of 14:07, 13 February 2013
Crystal Structure of a Genetically Modified Delta Class GST (adGSTD4-4) from Anopheles dirus, F123A, in Complex with S-Hexyl GlutathioneCrystal 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 StructureAbout this Structure
3f6d is a 2 chain structure with sequence from Anopheles dirus. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ 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