Cell adhesion molecule CEACAM1 (CEACAM1) is a 526-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P13688.
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The mean pLDDT of this model is 81.6 (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 | 64% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 18% |
What pLDDT means and how to read it
Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and also functions as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils (PubMed:18424730, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule…
Monomer. Oligomer. Heterodimer. Homodimer (PubMed:26483485). Cis-dimer/oligomer (via Ig-like C2-type and/or via cytoplasmic domains); induced by trans-homophilic cell adhesion through an allosteric mechanism transmitted by the Ig-like V-type domain, and is regulated by intracellular calcium and calmodulin. Interacts (via cytoplasmic domain) with calmodulin in a calcium dependent manner; reduces…
Cell membrane, Lateral cell membrane, Apical cell membrane, Basal cell membrane, Cell junction, Cell junction, adherens junction, Secreted, Cytoplasmic vesicle, secretory vesicle membrane, Cell projection, microvillus membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7MU8 | X-ray | 1.7 Å | A/B=35-141 |
| 6XO1 | X-ray | 1.76 Å | A/B=35-141 |
| 6XNO | X-ray | 1.9 Å | A/B=35-141 |
| 6XNW | X-ray | 1.9 Å | A/B/C/D=35-141 |
| 4QXW | X-ray | 2.04 Å | A/B=35-141 |
| 9U94 | EM | 2.11 Å | D/E/F=35-141 |
| 2GK2 | X-ray | 2.2 Å | A/B=32-141 |
| 7RPP | X-ray | 2.2 Å | A/B/C=35-141 |
| 4WHD | X-ray | 2.5 Å | A/B=34-141 |
| 6GBH | X-ray | 2.59 Å | B/D=35-142 |
| 6AW2 | X-ray | 2.68 Å | A=34-141 |
| 9GH5 | EM | 2.7 Å | D/E/F=35-428 |
| 6GBG | X-ray | 2.8 Å | D=35-142 |
| 9GH6 | EM | 3.0 Å | D=1-428 |
| 8CXJ | X-ray | 3.05 Å | A/C/E/G=34-141 |
| 6XNT | X-ray | 3.1 Å | A/B=35-141 |
| 6V3P | X-ray | 3.25 Å | A/B=34-141 |
| 5DZL | X-ray | 3.4 Å | A/B/C/D=35-141 |
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