Protein E6 (E6) is a 158-residue protein from Human papillomavirus type 16. This is its AlphaFold structure prediction, created 3 Jul 2025. UniProt accession: P03126.
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The mean pLDDT of this model is 91.2 (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 | 86% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents…
Forms homodimers. Interacts with ubiquitin-protein ligase UBE3A/E6-AP and thus forms a complex with human TP53. Interacts with human NFX1 and MAGI3. Interacts with human IRF3; this interaction inhibits the establishment of antiviral state. Interacts with human TYK2; this interaction inhibits JAK-STAT activation by interferon alpha. Interacts with host DLG1; this interaction leads to the…
Host cytoplasm, Host nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6SJA | X-ray | 1.5 Å | B=7-158 |
| 6SIV | X-ray | 1.75 Å | B=6-158 |
| 4JOP | X-ray | 1.8 Å | C/D=152-158 |
| 8B87 | X-ray | 2.0 Å | C/D=149-158 |
| 6HKS | X-ray | 2.19 Å | G/H/I/J/K/L=148-158 |
| 4XR8 | X-ray | 2.25 Å | F/H=8-158 |
| 6TWX | X-ray | 2.3 Å | C/D=149-158 |
| 6TWU | X-ray | 2.4 Å | C=149-158 |
| 8B9T | X-ray | 2.5 Å | B=149-158 |
| 4GIZ | X-ray | 2.55 Å | C/D=9-150 |
| 8JRN | EM | 2.6 Å | B/D=1-158 |
| 6TWQ | X-ray | 2.65 Å | C/D=149-158 |
| 7VZE | X-ray | 2.88 Å | E/F/G/H=152-158 |
| 8JRO | EM | 3.01 Å | B/D=1-158 |
| 7UAJ | X-ray | 3.25 Å | A/B/C/D=8-158 |
| 8GCR | EM | 3.38 Å | A=1-158 |
| 9CHT | EM | 3.54 Å | C=8-158 |
| 8JRP | EM | 3.58 Å | B/D=9-149 |
| 8R1F | EM | 3.67 Å | B=1-158 |
| 8R1G | EM | 3.99 Å | B/E=1-158 |
Showing 20 of 27 experimental structures (best resolution first).
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