Solution NMR structure of MAVS CARD. Determined by solution NMR. Released 2 Sept 2015.
Explore 2MS8 in 3D Show helices and sheets RCSB PDB PDBe
2MS8 contains 8 α-helices and 0 β-strands across 1 chain. 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 | 4-13 | 10 | |
| α-helix | 16-19 | 4 | |
| α-helix | 24-27 | 4 | |
| α-helix | 28-30 | 3 | |
| α-helix | 36-48 | 13 | |
| α-helix | 52-62 | 11 | |
| α-helix | 68-78 | 11 | |
| α-helix | 82-92 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitochondrial antiviral-signaling protein | A | protein | 102 | Homo sapiens | Q7Z434 (AlphaFold model) |
>2MS8_1 Mitochondrial antiviral-signaling protein (chains A) 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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