3ka6
From Proteopedia
(Difference between revisions)
m (Protected "3ka6" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
[[Image:3ka6.png|left|200px]] | [[Image:3ka6.png|left|200px]] | ||
- | <!-- | ||
- | The line below this paragraph, containing "STRUCTURE_3ka6", creates the "Structure Box" on the page. | ||
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
- | or leave the SCENE parameter empty for the default display. | ||
- | --> | ||
{{STRUCTURE_3ka6| PDB=3ka6 | SCENE= }} | {{STRUCTURE_3ka6| PDB=3ka6 | SCENE= }} | ||
===Frog M-ferritin, EED mutant, with cobalt=== | ===Frog M-ferritin, EED mutant, with cobalt=== | ||
- | |||
- | <!-- | ||
- | The line below this paragraph, {{ABSTRACT_PUBMED_20866049}}, adds the Publication Abstract to the page | ||
- | (as it appears on PubMed at http://www.pubmed.gov), where 20866049 is the PubMed ID number. | ||
- | --> | ||
{{ABSTRACT_PUBMED_20866049}} | {{ABSTRACT_PUBMED_20866049}} | ||
Line 22: | Line 11: | ||
==See Also== | ==See Also== | ||
- | *[[Ferritin]] | + | *[[Ferritin|Ferritin]] |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020866049</ref><references group="xtra"/> |
[[Category: Ferroxidase]] | [[Category: Ferroxidase]] | ||
[[Category: Rana catesbeiana]] | [[Category: Rana catesbeiana]] |
Revision as of 21:14, 25 July 2012
Contents |
Frog M-ferritin, EED mutant, with cobalt
Template:ABSTRACT PUBMED 20866049
About this Structure
3ka6 is a 1 chain structure of Ferritin with sequence from Rana catesbeiana. Full crystallographic information is available from OCA.
See Also
Reference
- Tosha T, Ng HL, Bhattasali O, Alber T, Theil EC. Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites. J Am Chem Soc. 2010 Oct 20;132(41):14562-9. PMID:20866049 doi:10.1021/ja105583d
Categories: Ferroxidase | Rana catesbeiana | Alber, T. | Bhattasali, O. | Ng, H L. | Theil, E. | Tosha, T. | Diiron | Iron | Iron storage | Metal-binding | Oxidoreductase