3rpp
From Proteopedia
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{{STRUCTURE_3rpp| PDB=3rpp | SCENE= }} | {{STRUCTURE_3rpp| PDB=3rpp | SCENE= }} | ||
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===Crystal structure of human kappa class glutathione transferase in apo form=== | ===Crystal structure of human kappa class glutathione transferase in apo form=== | ||
| + | {{ABSTRACT_PUBMED_21728995}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/GSTK1_HUMAN GSTK1_HUMAN]] Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB). | ||
==About this Structure== | ==About this Structure== | ||
[[3rpp]] is a 3 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=3RPP OCA]. | [[3rpp]] is a 3 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=3RPP OCA]. | ||
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| + | ==See Also== | ||
| + | *[[Glutathione S-transferase|Glutathione S-transferase]] | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:021728995</ref><references group="xtra"/><references/> | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 12:38, 3 July 2013
Contents |
Crystal structure of human kappa class glutathione transferase in apo form
Template:ABSTRACT PUBMED 21728995
Function
[GSTK1_HUMAN] Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB).
About this Structure
3rpp is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Wang B, Peng Y, Zhang T, Ding J. Crystal structures and kinetic studies of human Kappa class glutathione transferase provide insights into the catalytic mechanism. Biochem J. 2011 Oct 15;439(2):215-25. PMID:21728995 doi:10.1042/BJ20110753
