Ephrin type-A receptor 2 (EPHA2) is a 976-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29317.
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The mean pLDDT of this model is 82.3 (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 | 37% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A 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. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV…
Homodimer. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration (By similarity). Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation. Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form)…
Cell membrane, Cell projection, ruffle membrane, Cell projection, lamellipodium membrane, Cell junction, focal adhesion
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6Q7D | X-ray | 0.98 Å | A=596-900 |
| 6Q7B | X-ray | 1.01 Å | A=596-900 |
| 6FNG | X-ray | 1.04 Å | A=596-900 |
| 6Q7C | X-ray | 1.05 Å | A=596-900 |
| 6Q7G | X-ray | 1.05 Å | A=596-900 |
| 6Q7E | X-ray | 1.06 Å | A=596-900 |
| 5NKF | X-ray | 1.1 Å | A=596-900 |
| 5NKG | X-ray | 1.1 Å | A=596-900 |
| 8BOM | X-ray | 1.12 Å | A=596-900 |
| 6HES | X-ray | 1.13 Å | A=596-900 |
| 6Q7F | X-ray | 1.2 Å | A=596-900 |
| 6HET | X-ray | 1.21 Å | A=596-900 |
| 5I9Y | X-ray | 1.23 Å | A=596-900 |
| 5NK6 | X-ray | 1.27 Å | A=596-900 |
| 6HEW | X-ray | 1.27 Å | A=596-900 |
| 6HEV | X-ray | 1.28 Å | A=596-900 |
| 5NKH | X-ray | 1.29 Å | A=596-900 |
| 5NK5 | X-ray | 1.33 Å | A=596-900 |
| 5I9W | X-ray | 1.36 Å | A=596-900 |
| 6HEY | X-ray | 1.37 Å | A=596-900 |
Showing 20 of 103 experimental structures (best resolution first).
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