Envelope glycoprotein (GP) is a 676-residue protein from Zaire ebolavirus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: Q05320.
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The mean pLDDT of this model is 35.1 (very low 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 | 2% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 83% |
What pLDDT means and how to read it
Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion (PubMed:11836430). Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1 (PubMed:11112476). This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity) (Probable). Interacts with host…
Homotrimer; each monomer consists of a GP1 and a GP2 subunit linked by disulfide bonds (PubMed:35303429). The resulting peplomers (GP1,2) protrude from the virus surface as spikes. Interacts with host integrin alpha-V/ITGAV (PubMed:15596847). Interacts with host CLEC10A (PubMed:14990712). Also binds to host CD209 and CLEC4M/DC-SIGN(R) (PubMed:12050398, PubMed:12504546). Interacts with host FOLR1…
Virion membrane, Host cell membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2EBO | X-ray | 1.9 Å | A/B/C=557-630 |
| 6HS4 | X-ray | 2.05 Å | A=32-311, B=502-632 |
| 6F5U | X-ray | 2.07 Å | A=32-312, B=502-632 |
| 6F6N | X-ray | 2.15 Å | A=32-336 |
| 6G9I | X-ray | 2.19 Å | A=32-311, B=502-632 |
| 5JQ3 | X-ray | 2.23 Å | A=32-501, B=502-632 |
| 7SSQ | X-ray | 2.25 Å | A=32-336, B=502-632 |
| 6G9B | X-ray | 2.26 Å | A=32-311, B=502-632 |
| 7JPI | X-ray | 2.28 Å | A=1-293, B=502-637 |
| 6F6S | X-ray | 2.29 Å | A=32-336 |
| 6HRO | X-ray | 2.3 Å | A=32-312, B=502-632 |
| 6G95 | X-ray | 2.31 Å | A=32-311, B=502-632 |
| 7LYD | X-ray | 2.35 Å | A=32-318, B=502-632 |
| 6F6I | X-ray | 2.4 Å | A=32-336, B=502-632 |
| 7SSR | X-ray | 2.5 Å | A=32-336, B=502-632 |
| 8DPL | EM | 2.53 Å | D/I/M=33-312, E/J/N=502-637 |
| 9NNU | X-ray | 2.59 Å | A=32-501, B=502-632 |
| 8F87 | X-ray | 2.6 Å | A=32-318, B=502-632 |
| 5JQB | X-ray | 2.68 Å | A=32-501, B=502-632 |
| 5JQ7 | X-ray | 2.69 Å | A=32-501, B=502-632 |
Showing 20 of 55 experimental structures (best resolution first).
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