Pre-glycoprotein polyprotein GP complex (GPC) is a 491-residue protein from Lassa virus. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P08669.
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The mean pLDDT of this model is 62.8 (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 | 36% |
| 50 to 70 | Low: treat with caution | 41% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C) (PubMed:35173332). Helps to stabilize the spike complex in its native conformation (PubMed:35173332). The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion (PubMed:14555961)
Interacts with glycoprotein G2 (PubMed:14555961, PubMed:35173332). Part of the GP complex (GP-C) together with glycoprotein G1 and glycoprotein G2 (PubMed:35173332). The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding (By similarity)
Virion membrane, Host endoplasmic reticulum membrane, Host Golgi apparatus membrane, Host cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9MJ1 | EM | 1.9 Å | A/B/C=1-259, a/b/c=260-491 |
| 9MHE | EM | 2.01 Å | A/B/C=1-259, a/b/c=260-491 |
| 9MIV | EM | 2.02 Å | A/B/C=1-259, a/b/c=260-491 |
| 5OMI | X-ray | 2.56 Å | A/B/C=306-419 |
| 9MJ2 | EM | 2.58 Å | A/B/C=59-259, a/b/c=260-491 |
| 4ZJF | X-ray | 2.6 Å | A/B/C/D=75-237 |
| 7S8H | X-ray | 2.7 Å | A=59-259, a=260-424 |
| 9MIY | EM | 2.72 Å | A/B/C=1-58, a/b/c=260-491 |
| 7UOV | EM | 2.75 Å | A/B/C=1-259, a/b/c=260-491 |
| 7UOT | EM | 2.77 Å | A/B/C=1-259, a/b/c=260-491 |
| 7TYV | EM | 2.8 Å | A/B/C=1-259, a/b/c=260-423 |
| 8VCV | EM | 2.8 Å | A/B/C=1-259, a/b/c=260-424 |
| 8VE8 | EM | 2.8 Å | A/B/C=1-259, a/b/c=260-424 |
| 9CJ7 | EM | 3.0 Å | A/B/C=1-259, a/b/c=260-424 |
| 9CK8 | EM | 3.04 Å | A/B/C=1-259, a/b/c=260-424 |
| 5VK2 | X-ray | 3.2 Å | A/B/C=1-259, a/b/c=260-423 |
| 8EJJ | EM | 3.22 Å | A/B/C=59-255, a/b/c=260-423 |
| 7PUY | EM | 3.3 Å | A/B/C=1-259, a/b/c=260-491 |
| 8TYC | EM | 3.3 Å | A/B/C=1-259, a/b/c=260-423 |
| 9R8U | EM | 3.3 Å | A/B/C=1-259, a/b/c=260-491 |
Showing 20 of 34 experimental structures (best resolution first).
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