Tyrosine-protein kinase SYK (SYK) is a 635-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43405.
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The mean pLDDT of this model is 84.0 (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 | 63% |
| 70 to 90 | Confident: backbone generally right | 21% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development (PubMed:12387735, PubMed:33782605). Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains (PubMed:12387735, PubMed:9698567). The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM…
Interacts with LYN; phosphorylates SYK (By similarity). Interacts with RHOH (phosphorylated); regulates mast cells activation (By similarity). Interacts with NFAM1 (phosphorylated); probably involved in BCR signaling (By similarity). Interacts with VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR activation. Interacts with GAB2 (phosphorylated); probably involved in IgE Fc receptor signaling…
Cell membrane, Cytoplasm, cytosol
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4YJR | X-ray | 1.32 Å | A=355-635 |
| 4YJQ | X-ray | 1.34 Å | A=355-635 |
| 4FYO | X-ray | 1.4 Å | A=356-635 |
| 5LMA | X-ray | 1.43 Å | A=360-635 |
| 3BUW | X-ray | 1.45 Å | A/C=317-329 |
| 6ZCS | X-ray | 1.47 Å | A=343-635 |
| 5TIU | X-ray | 1.49 Å | A=356-635 |
| 8XQ1 | X-ray | 1.5 Å | A/B=356-635 |
| 8BI2 | X-ray | 1.51 Å | A=343-635 |
| 4YJT | X-ray | 1.52 Å | A=355-635 |
| 1XBB | X-ray | 1.57 Å | A=356-635 |
| 4RX8 | X-ray | 1.59 Å | A=356-635 |
| 4PX6 | X-ray | 1.6 Å | A=356-635 |
| 4YJO | X-ray | 1.6 Å | A=355-635 |
| 8RRQ | X-ray | 1.6 Å | A=355-635 |
| 6HM7 | X-ray | 1.64 Å | A=360-635 |
| 4YJV | X-ray | 1.65 Å | A=355-635 |
| 6ZCX | X-ray | 1.66 Å | A=343-635 |
| 4YJU | X-ray | 1.67 Å | A=355-635 |
| 4I0T | X-ray | 1.7 Å | A=356-635 |
Showing 20 of 93 experimental structures (best resolution first).
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