Protein C-ets-1 (ETS1) is a 441-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P14921.
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The mean pLDDT of this model is 65.4 (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 | 30% |
| 70 to 90 | Confident: backbone generally right | 19% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 44% |
What pLDDT means and how to read it
Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518)
Binds DNA as a homodimer; homodimerization is required for transcription activation (PubMed:18566588). Interacts with MAF and MAFB (By similarity). Interacts with PAX5; the interaction alters DNA-binding properties (By similarity). Interacts with DAXX (PubMed:10698492). Interacts with UBE2I (PubMed:9333025). Interacts with SP100; the interaction is direct and modulates ETS1 transcriptional…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1GVJ | X-ray | 1.53 Å | A/B=297-441 |
| 4LG0 | X-ray | 2.19 Å | B=331-440 |
| 4L18 | X-ray | 2.3 Å | B/F=296-441 |
| 3WTS | X-ray | 2.35 Å | C/H=276-441 |
| 3WTT | X-ray | 2.35 Å | C/H=276-441 |
| 3WU1 | X-ray | 2.4 Å | B=333-441 |
| 4L0Y | X-ray | 2.5 Å | B=296-441 |
| 2NNY | X-ray | 2.58 Å | A/B=280-441 |
| 3WU0 | X-ray | 2.6 Å | A/B=276-441 |
| 3WTZ | X-ray | 2.61 Å | A/B=276-441 |
| 3WTU | X-ray | 2.7 Å | C/H=276-441 |
| 3WTV | X-ray | 2.7 Å | C/H=276-441 |
| 3WTY | X-ray | 2.7 Å | C/H=276-441 |
| 4L0Z | X-ray | 2.7 Å | B=296-441 |
| 3WTX | X-ray | 2.8 Å | C/H=276-441 |
| 3WTW | X-ray | 2.9 Å | C/H=276-441 |
| 5ZMC | X-ray | 2.99 Å | B=331-441 |
| 3MFK | X-ray | 3.0 Å | A/B=280-441 |
| 3RI4 | X-ray | 3.0 Å | A/D=280-441 |
| 2STT | NMR | A=320-415 |
Showing 20 of 21 experimental structures (best resolution first).
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