T-cell surface glycoprotein CD3 zeta chain (CD247) is a 164-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20963.
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The mean pLDDT of this model is 62.4 (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 | 9% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 59% |
| Below 50 | Very low: often disordered regions | 17% |
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. 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. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways (PubMed:1384049, PubMed:1385158, PubMed:2470098, PubMed:7509083). CD247/CD3Z ITAMs phosphorylation creates multiple…
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. In turn, the hexamer interacts with CD247/CD3Z homodimer to form the TCR-CD3 complex. Alternatively, TCRalpha and TCRbeta can be replaced by TCRgamma and TCRdelta (PubMed:17055436). Interacts…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2OQ1 | X-ray | 1.9 Å | B=69-87 |
| 3IK5 | X-ray | 2.05 Å | B/D=63-80 |
| 8ES8 | EM | 2.65 Å | Y/Z=1-164 |
| 4XZ1 | X-ray | 2.8 Å | B=69-87 |
| 1YGR | X-ray | 2.9 Å | C/D=80-85 |
| 7FJE | EM | 3.0 Å | a/b=1-164 |
| 9CI8 | EM | 3.01 Å | a/b=27-57 |
| 8ES7 | EM | 3.04 Å | Y/Z=1-164 |
| 7PHR | EM | 3.08 Å | Z/z=22-57 |
| 9JY1 | EM | 3.08 Å | A/B/a/b=1-164 |
| 7FJF | EM | 3.1 Å | a/b=1-164 |
| 8TW6 | EM | 3.1 Å | X/Y=1-164 |
| 9IRU | EM | 3.14 Å | a/b=1-164 |
| 9IRS | EM | 3.18 Å | a/b=1-164 |
| 7FJD | EM | 3.2 Å | a/b=1-164 |
| 9JY2 | EM | 3.24 Å | a/b=26-56 |
| 8ES9 | EM | 3.25 Å | Y/Z=1-164 |
| 9CQ4 | EM | 3.27 Å | Y/Z=1-164 |
| 9JY4 | EM | 3.29 Å | A/B/a/b=1-164 |
| 8TW4 | EM | 3.3 Å | X/Y=1-164 |
Showing 20 of 38 experimental structures (best resolution first).
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