Genome polyprotein is a 126-residue protein from Zika virus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: A0A024B7W1.
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The mean pLDDT of this model is 71.8 (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 | 0% |
| 70 to 90 | Confident: backbone generally right | 57% |
| 50 to 70 | Low: treat with caution | 40% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of the mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Inhibits the integrated stress response (ISR) in the infected cell (PubMed:28592527)
Homodimer (By similarity). Interacts with host SERTAD3; this interaction promotes capsid protein C degradation (PubMed:36594413). Interacts with host CAPRIN1; this interaction is probably linked to the inhibition of stress granules formation by the virus (PubMed:28592527). Interacts with host G3BP1; this interaction is probably linked to the inhibition of stress granules formation by the virus…
Virion, Host nucleus, Host cytoplasm, Host cytoplasm, host perinuclear region, Host nucleus, host nucleolus, Secreted, Virion membrane, Host endoplasmic reticulum membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5KQR | X-ray | 1.33 Å | A=2521-2786 |
| 6LD1 | X-ray | 1.4 Å | A=2790-3411 |
| 6LD2 | X-ray | 1.4 Å | A=2790-3411 |
| 5KQS | X-ray | 1.5 Å | A=2521-2786 |
| 6LD4 | X-ray | 1.5 Å | A=2790-3411 |
| 6S0J | X-ray | 1.5 Å | A=1685-2125 |
| 5ULP | X-ray | 1.55 Å | A/B=2521-2788 |
| 5Y6N | X-ray | 1.57 Å | A=1682-2119 |
| 7M1V | X-ray | 1.6 Å | A/B=1420-1466, A/B=1504-1661 |
| 5KVE | X-ray | 1.7 Å | E=588-697 |
| 6RWZ | X-ray | 1.7 Å | A=1685-2125 |
| 5JMT | X-ray | 1.8 Å | A=1674-2119 |
| 5MRK | X-ray | 1.9 Å | A/B=2521-2784 |
| 6LD5 | X-ray | 1.94 Å | A=2790-3411 |
| 5NJV | X-ray | 2.0 Å | A/B/C/D=2524-2785 |
| 5Y6M | X-ray | 2.0 Å | A=1682-2119 |
| 5M5B | X-ray | 2.01 Å | A/B=2525-2786 |
| 5GOZ | X-ray | 2.05 Å | A/B/C=2524-2785 |
| 5NJU | X-ray | 2.1 Å | A/B=2525-2784 |
| 7A3N | X-ray | 2.1 Å | A=291-699 |
Showing 20 of 65 experimental structures (best resolution first).
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