2pvq: Difference between revisions
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[[Image:2pvq.png|left|200px]] | [[Image:2pvq.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
[[2pvq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVQ OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:018076047</ref><references group="xtra"/> | ||
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Ochrobactrum anthropi]] | [[Category: Ochrobactrum anthropi]] | ||
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[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Xenobiotics detoxification]] | [[Category: Xenobiotics detoxification]] | ||
Revision as of 10:44, 14 December 2011
Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site
Template:ABSTRACT PUBMED 18076047
About this Structure
2pvq is a 1 chain structure with sequence from Ochrobactrum anthropi. Full crystallographic information is available from OCA.
Reference
- Allocati N, Federici L, Masulli M, Favaloro B, Di Ilio C. Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site. Proteins. 2007 Dec 12;71(1):16-23. PMID:18076047 doi:10.1002/prot.21835
