3ph2
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | [[Image:3ph2.jpg|left|200px]] | |
| - | The | + | <!-- |
| + | The line below this paragraph, containing "STRUCTURE_3ph2", 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_3ph2| PDB=3ph2 | SCENE= }} | ||
| - | + | ===Structure of the imidazole-adduct of the Phormidium laminosum cytochrome c6 Q51V variant=== | |
| - | Description: Structure of the imidazole-adduct of the Phormidium laminosum cytochrome c6 Q51V variant | ||
| - | + | <!-- | |
| + | The line below this paragraph, {{ABSTRACT_PUBMED_21267610}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 21267610 is the PubMed ID number. | ||
| + | --> | ||
| + | {{ABSTRACT_PUBMED_21267610}} | ||
| + | |||
| + | ==About this Structure== | ||
| + | [[3ph2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phormidium_laminosum Phormidium laminosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PH2 OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:21267610</ref><references group="xtra"/> | ||
| + | [[Category: Phormidium laminosum]] | ||
| + | [[Category: Worrall, J A.R.]] | ||
Revision as of 06:11, 9 February 2011
Structure of the imidazole-adduct of the Phormidium laminosum cytochrome c6 Q51V variant
Template:ABSTRACT PUBMED 21267610
About this Structure
3ph2 is a 1 chain structure with sequence from Phormidium laminosum. Full crystallographic information is available from OCA.
Reference
- Rajagopal BS, Wilson MT, Bendall DS, Howe CJ, Worrall JA. Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue. J Biol Inorg Chem. 2011 Jan 26. PMID:21267610 doi:10.1007/s00775-011-0758-y
