Cadherin-1 (CDH1) is a 882-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P12830.
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The mean pLDDT of this model is 79.2 (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 | 47% |
| 70 to 90 | Confident: backbone generally right | 29% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via…
Homodimer; disulfide-linked (PubMed:11856755). Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions (PubMed:16126725, PubMed:7982500). Found in a complex composed of CDH1, RAP1A and PKP3; PKP3 acts as a scaffold protein within the…
Cell junction, adherens junction, Cell membrane, Endosome, Golgi apparatus, trans-Golgi network, Cytoplasm, Cell junction, desmosome, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2OMZ | X-ray | 1.6 Å | B=156-254 |
| 2OMX | X-ray | 1.7 Å | B=156-258 |
| 2OMY | X-ray | 1.7 Å | B=156-254 |
| 1O6S | X-ray | 1.8 Å | B=155-255 |
| 2OMU | X-ray | 1.8 Å | B=156-255 |
| 3FF7 | X-ray | 1.8 Å | A/B=155-253 |
| 2OMV | X-ray | 1.9 Å | B=156-255 |
| 8H62 | X-ray | 1.91 Å | B=155-367 |
| 4ZT1 | X-ray | 1.92 Å | A/B=157-367 |
| 2O72 | X-ray | 2.0 Å | A=155-367 |
| 2OMT | X-ray | 2.0 Å | B=156-255 |
| 3FF8 | X-ray | 2.0 Å | A/B=155-254 |
| 4ZTE | X-ray | 2.13 Å | A/B=157-367 |
| 6CXY | X-ray | 2.2 Å | C=155-371 |
| 3L6X | X-ray | 2.4 Å | B=756-773 |
| 6VEL | X-ray | 2.65 Å | C=155-371 |
| 7STZ | X-ray | 2.95 Å | C/D=155-698 |
| 3L6Y | X-ray | 3.0 Å | B/D/F=756-773 |
| 6OLE | EM | 3.1 Å | y=693-730 |
| 9P99 | EM | 3.37 Å | C=155-371 |
Showing 20 of 22 experimental structures (best resolution first).
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