Tyrosine-protein kinase Fyn (FYN) is a 537-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P06241.
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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 | 58% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance (PubMed:11536198, PubMed:15489916, PubMed:15557120, PubMed:16387660, PubMed:20100835, PubMed:7568038, PubMed:7822789). Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain (PubMed:15489916). Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions (PubMed:15489916). Involved in the regulation of cell adhesion…
Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB1, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity). Interacts with TOM1L1 (phosphorylated form). Interacts with KDR (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2…
Cytoplasm, Nucleus, Cell membrane, Perikaryon
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7A2P | X-ray | 0.9 Å | A=83-143 |
| 7A2X | X-ray | 0.92 Å | A=83-142 |
| 7A2O | X-ray | 0.94 Å | A=83-142 |
| 7A2Q | X-ray | 0.94 Å | A=83-143 |
| 7A2Y | X-ray | 0.97 Å | A=83-142 |
| 7A2W | X-ray | 0.99 Å | A=83-142 |
| 8KDX | X-ray | 1.01 Å | A=85-142 |
| 7A2S | X-ray | 1.02 Å | A=83-143 |
| 7A2R | X-ray | 1.05 Å | A=83-143 |
| 7A2Z | X-ray | 1.14 Å | A=83-142 |
| 7A2T | X-ray | 1.22 Å | A=83-143 |
| 6IPY | X-ray | 1.34 Å | A=82-144 |
| 4U1P | X-ray | 1.4 Å | A=148-248 |
| 6EDF | X-ray | 1.4 Å | A=83-146 |
| 7A2N | X-ray | 1.4 Å | A/B/C/D=83-142 |
| 9GHK | X-ray | 1.42 Å | A/B=80-143 |
| 3UA7 | X-ray | 1.5 Å | A/B/C/D=81-143 |
| 7A2J | X-ray | 1.5 Å | A/B=83-142 |
| 7A2K | X-ray | 1.5 Å | A/B/C/D=83-142 |
| 7A2M | X-ray | 1.5 Å | A/B=83-142 |
Showing 20 of 53 experimental structures (best resolution first).
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