Insulin-like growth factor 1 receptor (IGF1R) is a 1367-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08069.
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The mean pLDDT of this model is 78.0 (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 | 44% |
| 70 to 90 | Confident: backbone generally right | 32% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the…
Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chain carries the kinase domain. Interacts with PIK3R1 and with the PTB/PID domains of IRS1 and SHC1 in vitro when autophosphorylated on tyrosine residues. Forms a hybrid receptor with INSR, the hybrid is a tetramer consisting of 1 alpha chain…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1P4O | X-ray | 1.5 Å | A/B=973-1294 |
| 8PYN | X-ray | 1.71 Å | AAA=974-1286 |
| 3LW0 | X-ray | 1.79 Å | A/B/C/D=983-1286 |
| 5FXS | X-ray | 1.9 Å | A=980-1286 |
| 2OJ9 | X-ray | 2.0 Å | A=982-1286 |
| 3I81 | X-ray | 2.08 Å | A=982-1286 |
| 1JQH | X-ray | 2.1 Å | A/B/C=979-1286 |
| 1K3A | X-ray | 2.1 Å | A=988-1286 |
| 3O23 | X-ray | 2.1 Å | A=982-1286 |
| 4D2R | X-ray | 2.1 Å | A=985-1286 |
| 3NW7 | X-ray | 2.11 Å | A=982-1286 |
| 3NW5 | X-ray | 2.14 Å | A=982-1286 |
| 3NW6 | X-ray | 2.2 Å | A=982-1286 |
| 5HZN | X-ray | 2.2 Å | A/B/C/D/E/F/G/H=983-1286 |
| 8PYK | X-ray | 2.23 Å | AAA=974-1286 |
| 3D94 | X-ray | 2.3 Å | A=986-1286 |
| 5FXQ | X-ray | 2.3 Å | A=980-1286 |
| 5FXR | X-ray | 2.4 Å | A=980-1286 |
| 2ZM3 | X-ray | 2.5 Å | A/B/C/D=981-1286 |
| 1IGR | X-ray | 2.6 Å | A=31-492 |
Showing 20 of 46 experimental structures (best resolution first).
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