T-cell surface glycoprotein CD3 epsilon chain (CD3E) is a 207-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07766.
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The mean pLDDT of this model is 73.1 (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 | 28% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 28% |
| Below 50 | Very low: often disordered regions | 15% |
What pLDDT means and how to read it
Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response (PubMed:15294938, PubMed:15546002, PubMed:2470098, PubMed:40592325, PubMed:8490660). When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD247/CD3Z (PubMed:2470098, PubMed:40592325). All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain (PubMed:2470098, PubMed:40592325). Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the…
The TCR-CD3 complex is composed of a CD3D-CD3E and a CD3G-CD3E heterodimers that preferentially associate with TCRalpha and TCRbeta, respectively, to form TCRalpha-CD3E-CD3G and TCRbeta/CD3G-CD3E trimers (PubMed:15136729, PubMed:15534202, PubMed:40592325). In turn, the hexamer interacts with CD247/CD3Z homodimer to form the TCR-CD3 complex (PubMed:15136729, PubMed:15534202). Alternatively,…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5QU2 | X-ray | 1.04 Å | D/E=180-188 |
| 8VY4 | X-ray | 1.7 Å | C=22-28 |
| 8F0L | X-ray | 1.81 Å | P/Q=22-34 |
| 1XIW | X-ray | 1.9 Å | A/E=22-126 |
| 1SY6 | X-ray | 2.1 Å | A=21-118 |
| 8ES8 | EM | 2.65 Å | E/F=2-207 |
| 1A81 | X-ray | 3.0 Å | B/D/F/H/J/L=186-203 |
| 7FJE | EM | 3.0 Å | e/f=1-207 |
| 9CI8 | EM | 3.01 Å | e/f=33-156 |
| 8ES7 | EM | 3.04 Å | E/F=2-207 |
| 7PHR | EM | 3.08 Å | E/e=23-158 |
| 9JY1 | EM | 3.08 Å | E/F/e/f=1-207 |
| 7FJF | EM | 3.1 Å | e/f=1-207 |
| 8TW6 | EM | 3.1 Å | E/F=1-207 |
| 9IRU | EM | 3.14 Å | e/f=1-207 |
| 9IRS | EM | 3.18 Å | e/f=1-207 |
| 7FJD | EM | 3.2 Å | e/f=1-207 |
| 9JY2 | EM | 3.24 Å | e/f=33-154 |
| 8ES9 | EM | 3.25 Å | E/F=2-207 |
| 9CQ4 | EM | 3.27 Å | E/F=1-207 |
Showing 20 of 43 experimental structures (best resolution first).
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