Mitochondrial antiviral-signaling protein (MAVS) is a 540-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q7Z434.
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The mean pLDDT of this model is 54.9 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 17% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 64% |
What pLDDT means and how to read it
Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970, PubMed:39589880, PubMed:38995016). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243,…
Self-associates and polymerizes (via CARD domains) to form 400 nM long three-stranded helical filaments on mitochondria, filament nucleation requires interaction with RIGI whose CARD domains act as a template for filament assembly (PubMed:24569476, PubMed:25018021, PubMed:27992402, PubMed:26246171). Interacts with RIGI, IFIH1/MDA5, TRAF2, TRAF6 and C1QBP (PubMed:16125763, PubMed:16127453,…
Mitochondrion outer membrane, Mitochondrion, Peroxisome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3RC5 | X-ray | 1.6 Å | B=502-508 |
| 2VGQ | X-ray | 2.1 Å | A=3-93 |
| 5JEK | X-ray | 2.4 Å | C/D=433-450 |
| 4Z8M | X-ray | 2.95 Å | C/D=450-468 |
| 7DNI | EM | 3.2 Å | M/N/O/P=1-97 |
| 8WKW | EM | 3.21 Å | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-97 |
| 4P4H | X-ray | 3.4 Å | I/J/K/L/M/N/O/P=1-99 |
| 3J6J | EM | 3.64 Å | A/B/C/D/E/G/I/L=1-97 |
| 3J6C | EM | 9.6 Å | A=3-93 |
| 2MS7 | NMR | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=1-100 | |
| 2MS8 | NMR | A=1-100 |
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