Fibroblast growth factor receptor 1 (FGFR1) is a 822-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P11362.
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The mean pLDDT of this model is 73.9 (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 | 34% |
| 70 to 90 | Confident: backbone generally right | 36% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 23% |
What pLDDT means and how to read it
Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers…
Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro) (PubMed:12181353, PubMed:16597617, PubMed:1697263, PubMed:1722683, PubMed:17623664, PubMed:8663044, PubMed:9655399). Ligand specificity is determined by tissue-specific expression of isoforms, and differences…
Cell membrane, Nucleus, Cytoplasm, cytosol, Cytoplasmic vesicle
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5EW8 | X-ray | 1.63 Å | A/B=458-765 |
| 4WUN | X-ray | 1.65 Å | A/B=459-765 |
| 9U7G | X-ray | 1.66 Å | A/B=458-765 |
| 7OZB | X-ray | 1.71 Å | AAA/BBB=458-765 |
| 8XZ7 | X-ray | 1.75 Å | A/B=458-765 |
| 9UHI | X-ray | 1.76 Å | A/B=458-765 |
| 9VLJ | X-ray | 1.81 Å | A/B=458-765 |
| 7OZD | X-ray | 1.82 Å | AAA/BBB=458-765 |
| 7OZF | X-ray | 1.82 Å | AAA/BBB=458-765 |
| 9UHC | X-ray | 1.88 Å | A/B=458-765 |
| 5O49 | X-ray | 1.91 Å | A/B=458-765 |
| 3DPK | X-ray | 1.95 Å | A=577-615 |
| 4UWC | X-ray | 1.96 Å | A/B=458-765 |
| 5AM6 | X-ray | 1.96 Å | A/B=458-765 |
| 5AM7 | X-ray | 1.96 Å | A/B=458-765 |
| 6ITJ | X-ray | 1.99 Å | A/B=458-765 |
| 8JMZ | X-ray | 1.99 Å | A/B=458-765 |
| 1FGK | X-ray | 2.0 Å | A/B=456-765 |
| 4ZSA | X-ray | 2.0 Å | A/B=458-765 |
| 6C1B | X-ray | 2.0 Å | A/B=459-765 |
Showing 20 of 83 experimental structures (best resolution first).
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