Polymerase cofactor VP35 (VP35) is a 340-residue protein from Zaire ebolavirus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: Q05127.
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The mean pLDDT of this model is 71.3 (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 | 32% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 17% |
| Below 50 | Very low: often disordered regions | 21% |
What pLDDT means and how to read it
Plays an essential role in viral RNA synthesis and also a role in suppressing innate immune signaling (PubMed:11027311, PubMed:35533195). Acts as a polymerase cofactor in the RNA polymerase transcription and replication complexes (PubMed:16495261, PubMed:24495995, PubMed:9971816). Serves as nucleoprotein/NP monomer chaperone prior to the formation of the large oligomeric RNA-bound complexes (By similarity). Part of the external layer of the nucleocapsid, likely tethering the nucleocapsid to the matrix and membrane (PubMed:39293445). Regulates RNA synthesis by modulating NP-RNA interactions and interacting with DYNLL1 (PubMed:25741013). VP35-NP interaction controls the switch between…
Homodimer (By similarity). Homotetramer or homotrimer; via the coiled coil domain (PubMed:16095644, PubMed:30482729, PubMed:40164610). Interacts with nucleoprotein NP and polymerase L; VP35 bridges L and NP and allows the formation of the polymerase complex (PubMed:40164610). Also interacts with VP30; this interaction is regulated by VP30 phosphorylation (PubMed:23493393). Interacts with host…
Virion, Host cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3FKE | X-ray | 1.4 Å | A/B=215-340 |
| 4IBG | X-ray | 1.41 Å | A/B=215-340 |
| 4IBI | X-ray | 1.47 Å | A/B=215-340 |
| 4IBJ | X-ray | 1.54 Å | A/B=215-340 |
| 3L29 | X-ray | 1.7 Å | A/B=215-340 |
| 4IBC | X-ray | 1.74 Å | A/B=215-340 |
| 4IBB | X-ray | 1.75 Å | A/B=215-340 |
| 4IBD | X-ray | 1.84 Å | A/B=215-340 |
| 4IBK | X-ray | 1.85 Å | A/B=215-340 |
| 4IJE | X-ray | 1.9 Å | A/B/C/D=218-340 |
| 3L27 | X-ray | 1.95 Å | A/B/C/D=215-340 |
| 4IBE | X-ray | 1.95 Å | A/B=215-340 |
| 3L25 | X-ray | 2.0 Å | A/B/D/E=215-340 |
| 6GBO | X-ray | 2.1 Å | A/B/C/D/E/F/G/H/I/J/K/L=82-145 |
| 4IBF | X-ray | 2.29 Å | A/B=215-340 |
| 3L26 | X-ray | 2.4 Å | A/B=215-340 |
| 3L28 | X-ray | 2.4 Å | A/B/C/D/E/F=215-340 |
| 4ZTA | X-ray | 2.4 Å | A=15-60 |
| 4ZTI | X-ray | 2.4 Å | A/B=15-60 |
| 4IJF | X-ray | 2.51 Å | A=218-340 |
Showing 20 of 26 experimental structures (best resolution first).
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