Proto-oncogene tyrosine-protein kinase Src (SRC) is a 533-residue protein from Gallus gallus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P00523.
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The mean pLDDT of this model is 84.1 (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 | 67% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors (By similarity). Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, cell apoptosis and transformation, cell migration, and bone remodeling (By similarity). Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC…
Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with GJA1 and PXN
Cell membrane, Mitochondrion inner membrane, Endosome membrane, Nucleus, Cytoplasm, cytoskeleton, Cell junction, focal adhesion, Cytoplasm, perinuclear region, Cell junction
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6XVM | X-ray | 0.9 Å | A/B/C/D=82-141 |
| 7A31 | X-ray | 0.94 Å | A/B=82-141 |
| 5OAV | X-ray | 0.95 Å | A/C=85-141 |
| 7A33 | X-ray | 0.96 Å | A/B=82-141 |
| 4HVU | X-ray | 0.98 Å | A=85-141 |
| 4HVW | X-ray | 0.98 Å | A=85-141 |
| 4RTZ | X-ray | 0.98 Å | A=85-141 |
| 4OMO | X-ray | 1.04 Å | A/B=85-141 |
| 6XX4 | X-ray | 1.05 Å | A=85-141 |
| 4HVV | X-ray | 1.1 Å | A=85-140 |
| 7A32 | X-ray | 1.15 Å | A/B/C/D=82-141 |
| 5ECA | X-ray | 1.16 Å | A=85-141 |
| 5OB0 | X-ray | 1.17 Å | A=85-141 |
| 5OB1 | X-ray | 1.17 Å | A=85-141 |
| 4RTW | X-ray | 1.24 Å | A/C=85-141 |
| 6XX2 | X-ray | 1.25 Å | A=85-141 |
| 4RTY | X-ray | 1.28 Å | A=85-141 |
| 6XX5 | X-ray | 1.3 Å | A=85-141 |
| 7A35 | X-ray | 1.31 Å | A/B=82-141 |
| 4RTX | X-ray | 1.32 Å | A/B/C/D=85-141 |
Showing 20 of 141 experimental structures (best resolution first).
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