Antiviral innate immune response receptor RIG-I (RIGI) is a 925-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O95786.
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The mean pLDDT of this model is 85.2 (confident 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 | 52% |
| 70 to 90 | Confident: backbone generally right | 39% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 6% |
What pLDDT means and how to read it
Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines (PubMed:15208624, PubMed:15708988, PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:24366338, PubMed:28469175, PubMed:29117565, PubMed:31006531, PubMed:34935440, PubMed:35263596, PubMed:36793726). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that…
Monomer; maintained as a monomer in an autoinhibited state. Upon binding of viral RNAs and conformational shift, homooligomerizes and forms filaments on these molecules (PubMed:26471729, PubMed:31881323). Interacts (via tandem CARD domain) with MAVS/IPS1 promoting its filamentation. Interacts with DHX58/LGP2, IKBKE, TBK1 and STING1. Interacts (via CARD domain) with TRIM25 (via SPRY domain).…
Cytoplasm, Cell projection, ruffle membrane, Cytoplasm, cytoskeleton, Cell junction, tight junction
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7BAH | X-ray | 1.89 Å | A/B=802-925 |
| 7MK1 | X-ray | 1.9 Å | A/B=801-925 |
| 3LRR | X-ray | 2.15 Å | A/B=803-923 |
| 3OG8 | X-ray | 2.4 Å | A/B=802-925 |
| 9KU4 | EM | 2.4 Å | B=1-925 |
| 2YKG | X-ray | 2.5 Å | A=230-925 |
| 3ZD7 | X-ray | 2.5 Å | A=230-925 |
| 3NCU | X-ray | 2.55 Å | A/B=792-925 |
| 4BPB | X-ray | 2.58 Å | A=230-925 |
| 3LRN | X-ray | 2.6 Å | A/B=803-923 |
| 5F9F | X-ray | 2.6 Å | A/C/E/G/I/K=232-925 |
| 9KTW | EM | 2.6 Å | B=1-925 |
| 2QFD | X-ray | 2.7 Å | A/B/C/D/E/F/G/H/I/J=802-925 |
| 5E3H | X-ray | 2.7 Å | A=232-925 |
| 4ON9 | X-ray | 2.71 Å | A/B=230-793 |
| 3ZD6 | X-ray | 2.8 Å | A=230-925 |
| 4AY2 | X-ray | 2.8 Å | A=239-925 |
| 6GPG | X-ray | 2.89 Å | A=232-925 |
| 8DVU | EM | 2.9 Å | A=1-925 |
| 2QFB | X-ray | 3.0 Å | A/B/C/D/E/F/G/H/I/J=802-925 |
Showing 20 of 44 experimental structures (best resolution first).
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