4F4L
Open Channel Conformation of a Voltage Gated Sodium Channel
Summary for 4F4L
Entry DOI | 10.2210/pdb4f4l/pdb |
Descriptor | Ion transport protein (2 entities in total) |
Functional Keywords | alpha helical membrane protein, voltage-gated sodium channel, membrane, metal transport |
Biological source | Magnetococcus marinus |
Total number of polymer chains | 4 |
Total formula weight | 49758.06 |
Authors | McCusker, E.C.,Bagneris, C.,Naylor, C.E.,Cole, A.R.,D'Avanzo, N.,Nichols, C.G.,Wallace, B.A. (deposition date: 2012-05-10, release date: 2012-10-03, Last modification date: 2023-09-13) |
Primary citation | McCusker, E.C.,Bagneris, C.,Naylor, C.E.,Cole, A.R.,D'Avanzo, N.,Nichols, C.G.,Wallace, B.A. Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing. Nat Commun, 3:1102-1102, 2012 Cited by PubMed: 23033078DOI: 10.1038/ncomms2077 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.49 Å) |
Structure validation
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