Genome polyprotein is a 122-residue protein from Hepatitis C virus genotype 1a. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P27958.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 90.3 (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 | 65% |
| 70 to 90 | Confident: backbone generally right | 33% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (PubMed:18033802). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma…
Homooligomer (PubMed:25351725). Interacts with E1 (via C-terminus) (PubMed:8764026). Interacts with the non-structural protein 5A (By similarity). Interacts (via N-terminus) with host STAT1 (via SH2 domain); this interaction results in decreased STAT1 phosphorylation and ubiquitin-mediated proteasome-dependent STAT1 degradation, leading to decreased IFN-stimulated gene transcription…
Host endoplasmic reticulum membrane, Host mitochondrion membrane, Virion, Host cytoplasm, Host nucleus, Host lipid droplet, Virion membrane, Host mitochondrion, Host cell membrane, Host cytoplasm, host perinuclear region
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3RC4 | X-ray | 1.5 Å | A=1026-1208 |
| 3RC5 | X-ray | 1.6 Å | A=1026-1208 |
| 6BZY | X-ray | 1.6 Å | B=412-423 |
| 5FGB | X-ray | 1.65 Å | F/G=405-425 |
| 6BQJ | X-ray | 1.69 Å | A/B/C=1030-1208 |
| 2XI3 | X-ray | 1.7 Å | A/B=2421-2990 |
| 4N0Y | X-ray | 1.75 Å | A=314-324 |
| 2XI2 | X-ray | 1.8 Å | A/B/C=2421-2990 |
| 5FGC | X-ray | 1.9 Å | A=405-425 |
| 6UYD | X-ray | 1.9 Å | E/F=412-645 |
| 6BQK | X-ray | 1.97 Å | A/B=1030-1208 |
| 5EOC | X-ray | 1.98 Å | P/Q=412-422 |
| 2O8M | X-ray | 2.0 Å | A/B=1027-1207, C/D=1678-1696 |
| 4XVJ | X-ray | 2.0 Å | A=412-423 |
| 4Z0X | X-ray | 2.0 Å | C=435-446 |
| 5YXN | X-ray | 2.03 Å | I=1406-1415 |
| 4JZN | X-ray | 2.05 Å | K=434-446 |
| 1HEI | X-ray | 2.1 Å | A/B=1206-1656 |
| 1A1V | X-ray | 2.2 Å | A=1193-1659 |
| 6BZW | X-ray | 2.2 Å | I/J/K/L=412-423 |
Showing 20 of 59 experimental structures (best resolution first).
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