Proto-oncogene tyrosine-protein kinase Src (SRC) is a 536-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P12931.
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The mean pLDDT of this model is 83.4 (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 | 66% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 16% |
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 (PubMed:34234773). Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be…
Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Interacts with DDEF1/ASAP1; via the SH3 domain (By similarity). Interacts with CCPG1 (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (By…
Cell membrane, Mitochondrion inner membrane, Nucleus, Cytoplasm, cytoskeleton, Cytoplasm, perinuclear region, Cell junction, focal adhesion, Cell junction
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9OFX | X-ray | 1.45 Å | A/B/C/D=85-143 |
| 1FMK | X-ray | 1.5 Å | A=86-536 |
| 1O43 | X-ray | 1.5 Å | A=145-252 |
| 1O4A | X-ray | 1.5 Å | A=145-252 |
| 1O4R | X-ray | 1.5 Å | A=145-252 |
| 2SRC | X-ray | 1.5 Å | A=86-536 |
| 6C4S | X-ray | 1.5 Å | A/B=87-144 |
| 7NG7 | X-ray | 1.5 Å | A=254-536 |
| 8VCF | X-ray | 1.5 Å | A=144-251 |
| 1O48 | X-ray | 1.55 Å | A=145-252 |
| 1O4G | X-ray | 1.55 Å | A=145-252 |
| 1O4K | X-ray | 1.57 Å | A=145-252 |
| 4F5B | X-ray | 1.57 Å | A=144-252 |
| 1O4M | X-ray | 1.6 Å | A=145-252 |
| 1O4N | X-ray | 1.6 Å | A=145-252 |
| 8VCG | X-ray | 1.61 Å | A=144-250 |
| 1O4L | X-ray | 1.65 Å | A=145-252 |
| 1O41 | X-ray | 1.7 Å | A=145-252 |
| 1O42 | X-ray | 1.7 Å | A=145-252 |
| 1O44 | X-ray | 1.7 Å | A=145-252 |
Showing 20 of 79 experimental structures (best resolution first).
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