4ma9
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
{{STRUCTURE_4ma9| PDB=4ma9 | SCENE= }} | {{STRUCTURE_4ma9| PDB=4ma9 | SCENE= }} | ||
===Wild type Salmonella Alkyl Hydroperoxide Reductase C in its substrate-ready conformation=== | ===Wild type Salmonella Alkyl Hydroperoxide Reductase C in its substrate-ready conformation=== | ||
| + | {{ABSTRACT_PUBMED_24175952}} | ||
==Function== | ==Function== | ||
| Line 6: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | [[4ma9]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MA9 OCA]. | + | [[4ma9]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MA9 OCA]. |
| + | |||
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:024175952</ref><references group="xtra"/><references/> | ||
| + | [[Category: Bacillus typhimurium loeffler 1892]] | ||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
[[Category: Karplus, P A.]] | [[Category: Karplus, P A.]] | ||
Revision as of 08:26, 27 November 2013
Contents |
Wild type Salmonella Alkyl Hydroperoxide Reductase C in its substrate-ready conformation
Template:ABSTRACT PUBMED 24175952
Function
[AHPC_SALTY] Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase.
About this Structure
4ma9 is a 5 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892. Full crystallographic information is available from OCA.
Reference
- Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA. Substrate-ready Conformation of Wild Type Salmonella typhimurium AhpC and the Sensitive Balance between Fully Folded and Locally Unfolded Conformations. Biochemistry. 2013 Oct 31. PMID:24175952 doi:http://dx.doi.org/10.1021/bi4011573
