Telomeric repeat-binding factor 2 (TERF2) is a 542-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15554.
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The mean pLDDT of this model is 68.0 (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 | 39% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 41% |
What pLDDT means and how to read it
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:15608617, PubMed:16166375, PubMed:20655466, PubMed:28216226, PubMed:31595153, PubMed:9326950, PubMed:9326951, PubMed:9476899). In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (PubMed:16166375, PubMed:20655466). Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (PubMed:16166375). Shelterin associates with arrays…
Homodimer (PubMed:15608617). Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP/RAP1, ACD and POT1 (PubMed:15316005, PubMed:15383534, PubMed:15608617, PubMed:18202258). Interacts with NBN; interaction takes place with unphosphorylated NBN during G1 phase and prevents to prevent ATM activation and non-homologous end joining repair (PubMed:10888888,…
Nucleus, Chromosome, telomere
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3SJM | X-ray | 1.35 Å | A/B=483-542 |
| 1W0U | X-ray | 1.8 Å | A/B=488-542 |
| 3K6G | X-ray | 1.95 Å | D/E/F=317-358 |
| 4M7C | X-ray | 2.05 Å | A/B=87-286 |
| 6J67 | X-ray | 2.05 Å | A=84-287 |
| 3BU8 | X-ray | 2.15 Å | A/B=84-318 |
| 7C5D | X-ray | 2.15 Å | A/B=84-287 |
| 1H6P | X-ray | 2.2 Å | A/B=85-287 |
| 5XYF | X-ray | 2.2 Å | C=392-408 |
| 4RQI | X-ray | 2.44 Å | A/B/C/D=85-287 |
| 3BUA | X-ray | 2.5 Å | A/B/C/D=84-287 |
| 9Q9K | EM | 2.59 Å | J/K=438-542 |
| 9Q9J | EM | 2.71 Å | J=438-542 |
| 9Q9M | EM | 2.81 Å | J=1-542 |
| 5WQD | X-ray | 3.0 Å | A/B/C/D/E/F/G=84-287 |
| 1VF9 | NMR | A=480-542 | |
| 1VFC | NMR | A=480-542 | |
| 1XG1 | NMR | A=480-542 |
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