High-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARD. Determined by solid-state NMR. Released 2 Sept 2015.
Explore 2MS7 in 3D Show helices and sheets RCSB PDB PDBe
2MS7 contains 147 α-helices and 0 β-strands across 21 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 | |
| α-helix | 16-19 | 4 | |
| α-helix | 24-26 | 3 | |
| α-helix | 36-48 | 13 | |
| α-helix | 51-61 | 11 | |
| α-helix | 69-78 | 10 | |
| α-helix | 82-93 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitochondrial antiviral-signaling protein | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U | protein | 102 | Homo sapiens | Q7Z434 (AlphaFold model) |
>2MS7_1 Mitochondrial antiviral-signaling protein (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U) GSMPFAEDKTYKYICRNFSNFCNVDVVEILPYLPCLTARDQDRLRATCTLSGNRDTLWHL FNTLQRRPGWVEYFIAALRGCELVDLADEVASVYQSYQPRTS
Structure determination of helical filaments by solid-state NMR spectroscopy. He, L., Bardiaux, B., Ahmed, M. et al. Proc Natl Acad Sci U S A (2016) 113:E272-E281. DOI 10.1073/pnas.1513119113 · PubMed
Other PDB entries of the same protein (UniProt Q7Z434 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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