Ephrin type-A receptor 3 (EPHA3) is a 983-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29320.
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The mean pLDDT of this model is 80.8 (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 | 53% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (PubMed:11870224, PubMed:12794130). Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5 (By similarity). Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration (PubMed:11870224). Also activated by EFNA1, inhibiting epithelial-to-mesenchymal transition of…
Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with NCK1 (via SH2 domain);…
Cell membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2QOL | X-ray | 1.07 Å | A=577-947 |
| 2QOD | X-ray | 1.15 Å | A=577-947 |
| 2QOF | X-ray | 1.2 Å | A=577-947 |
| 2QOK | X-ray | 1.2 Å | A=577-947 |
| 2QOC | X-ray | 1.25 Å | A=606-947 |
| 2QOI | X-ray | 1.25 Å | A=577-947 |
| 2QOO | X-ray | 1.25 Å | A=577-947 |
| 4P5Q | X-ray | 1.35 Å | A=606-947 |
| 6IN0 | X-ray | 1.5 Å | A=613-904 |
| 2QO9 | X-ray | 1.55 Å | A=577-947 |
| 2QO2 | X-ray | 1.6 Å | A=577-947 |
| 2QO7 | X-ray | 1.6 Å | A=577-947 |
| 2QOQ | X-ray | 1.6 Å | A=577-947 |
| 4P4C | X-ray | 1.6 Å | A=606-947 |
| 2QOB | X-ray | 1.65 Å | A=606-947 |
| 3FXX | X-ray | 1.7 Å | A=577-947 |
| 4G2F | X-ray | 1.7 Å | A=606-947 |
| 4TWN | X-ray | 1.71 Å | A=609-947 |
| 3DZQ | X-ray | 1.75 Å | A=606-947 |
| 2GSF | X-ray | 1.77 Å | A=577-947 |
Showing 20 of 28 experimental structures (best resolution first).
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