RNA directed RNA polymerase (ORF1) is a 510-residue protein from Norovirus. This is its AlphaFold structure prediction, created 3 Sept 2026. UniProt accession: Q80J95.
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The mean pLDDT of this model is 91.8 (very high 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 | 83% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Induces the proliferation of the host smooth ER membranes forming long tubular structures (By similarity). These remodeled membranes probably form the viral factories that contain the replication complex (By similarity). May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable)
Homodimer (PubMed:22347381). Interacts with NTPase; this interaction increases the proapoptotic activity of the NTPase and is crucial for the formation of the viral replication complex (By similarity). Interacts with NS4; this interaction is crucial for the formation of the viral replication complex (By similarity). Interacts (via N-terminus) with host VAPA (PubMed:28698274). Interacts with host…
Host endoplasmic reticulum membrane, Secreted, Host endosome membrane, Host mitochondrion, Host cytoplasm, host perinuclear region
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4ASH | X-ray | 1.58 Å | A/B=995-1177 |
| 3UQS | X-ray | 2.0 Å | A/B/C=1181-1687 |
| 3SFG | X-ray | 2.21 Å | A/B/C=1181-1686 |
| 4NRU | X-ray | 2.3 Å | A/B/C/D/E/F=1181-1687 |
| 4X2V | X-ray | 2.3 Å | A/B/C/D=995-1178, E=1174-1178 |
| 8A8X | X-ray | 2.37 Å | B/D=699-705 |
| 4O4R | X-ray | 2.4 Å | A/B/C=1181-1687 |
| 4X2Y | X-ray | 2.42 Å | A/B=998-1173 |
| 3UR0 | X-ray | 2.45 Å | A/B/C=1181-1687 |
| 4X2X | X-ray | 2.47 Å | A=998-1173 |
| 3QID | X-ray | 2.5 Å | A/B/C=1181-1686 |
| 3SFU | X-ray | 2.5 Å | A/B/C=1181-1686 |
| 3NAI | X-ray | 2.56 Å | A/B/C=1181-1686 |
| 3UPF | X-ray | 2.6 Å | A/B/C=1174-1687 |
| 4X2W | X-ray | 2.7 Å | A/B=997-1175 |
| 3NAH | X-ray | 2.75 Å | A/B/C=1181-1686 |
| 8A5M | X-ray | 2.92 Å | C/E=1171-1177 |
| 5Y3D | X-ray | 3.14 Å | A/B/C/D/E/F=1181-1686 |
| 2M4G | NMR | A=881-955 | |
| 2MCD | NMR | A=28-114 |
Showing 20 of 21 experimental structures (best resolution first).
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