Telomeric repeat-binding factor 1 (TERF1) is a 439-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P54274.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 71.1 (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 | 48% |
| 70 to 90 | Confident: backbone generally right | 10% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 36% |
What pLDDT means and how to read it
Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length (PubMed:31595153). Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways
Homodimer; can contain both isoforms. Found in a complex with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via N-terminus). Interacts with FBXO4. Interaction with TINF2 protects against interaction with FBXO4 and subsequent…
Nucleus, Cytoplasm, cytoskeleton, spindle, Chromosome, telomere
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9HCZ | X-ray | 1.55 Å | A=48-268 |
| 9HCX | X-ray | 1.69 Å | A=48-268 |
| 9HCP | X-ray | 1.7 Å | A=48-268 |
| 9HCT | X-ray | 1.7 Å | A=48-268 |
| 9HD1 | X-ray | 1.73 Å | A=48-268 |
| 9HCL | X-ray | 1.87 Å | A=48-268 |
| 9HD9 | X-ray | 1.87 Å | A=48-268 |
| 9HF9 | X-ray | 1.9 Å | A=48-268 |
| 9HCN | X-ray | 1.93 Å | A=48-268 |
| 9HCR | X-ray | 1.93 Å | A=48-268 |
| 9HCY | X-ray | 1.93 Å | A=48-268 |
| 9HD0 | X-ray | 1.93 Å | A=48-268 |
| 9HCQ | X-ray | 1.96 Å | A=48-268 |
| 1W0T | X-ray | 2.0 Å | A/B=379-431 |
| 3BQO | X-ray | 2.0 Å | A=58-268 |
| 9HFG | X-ray | 2.02 Å | A=48-268 |
| 9HFE | X-ray | 2.04 Å | A=48-268 |
| 9HFA | X-ray | 2.05 Å | A=48-268 |
| 9HFF | X-ray | 2.06 Å | A=48-268 |
| 9HCU | X-ray | 2.07 Å | A=48-268 |
Showing 20 of 58 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.