Telomerase reverse transcriptase (TERT) is a 1132-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O14746.
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The mean pLDDT of this model is 80.2 (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 | 58% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the…
Catalytic component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC) (PubMed:19179534, PubMed:20351177, PubMed:29695869). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1…
Nucleus, nucleolus, Nucleus, nucleoplasm, Nucleus, Chromosome, telomere, Cytoplasm, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5MEO | X-ray | 1.77 Å | C=540-548 |
| 5MER | X-ray | 1.88 Å | C/F=540-548 |
| 5MEQ | X-ray | 2.27 Å | C=540-548 |
| 5UGW | X-ray | 2.31 Å | A=961-1132 |
| 4B18 | X-ray | 2.52 Å | B=222-240 |
| 5MEP | X-ray | 2.71 Å | C/F=540-548 |
| 4MNQ | X-ray | 2.74 Å | C=540-548 |
| 2BCK | X-ray | 2.8 Å | C/F=461-469 |
| 5MEN | X-ray | 2.81 Å | C=540-548 |
| 7QXA | EM | 3.2 Å | A=1-1132 |
| 9SHZ | EM | 3.2 Å | A=1-1132 |
| 7TRD | EM | 3.3 Å | A=1-1132 |
| 9QAX | EM | 3.3 Å | A=1-1132 |
| 7TRE | EM | 3.5 Å | A=1-1132 |
| 9SHY | EM | 3.53 Å | A=1-1132 |
| 7V99 | EM | 3.54 Å | A=1-1132 |
| 9QAZ | EM | 3.6 Å | A=1-1132 |
| 7TRF | EM | 3.7 Å | A=1-1132 |
| 7BG9 | EM | 3.8 Å | A=1-1132 |
| 9QAY | EM | 3.8 Å | A=1-1132 |
Showing 20 of 23 experimental structures (best resolution first).
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