Fibroblast growth factor receptor 2 (FGFR2) is a 821-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P21802.
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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 | 37% |
| 70 to 90 | Confident: backbone generally right | 31% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 26% |
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 cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and…
Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in vitro). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Isoform 1 has high affinity for FGF1 and FGF2, but…
Cell membrane, Golgi apparatus, Cytoplasmic vesicle, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 10OU | X-ray | 1.77 Å | A/B=458-768 |
| 2PVF | X-ray | 1.8 Å | A=458-778, B=764-778 |
| 3B2T | X-ray | 1.8 Å | A/B=458-768 |
| 10OO | X-ray | 1.85 Å | A/B=458-768 |
| 4J99 | X-ray | 1.85 Å | A/B/C/D=458-768 |
| 5UGL | X-ray | 1.86 Å | A/B=458-768 |
| 3CAF | X-ray | 1.96 Å | A=150-249 |
| 10OQ | X-ray | 1.98 Å | A/B=458-768 |
| 9U7S | X-ray | 1.99 Å | A/B=465-768 |
| 3CLY | X-ray | 2.0 Å | A=458-778 |
| 8W3D | X-ray | 2.04 Å | A/B/C/D=458-768 |
| 5UI0 | X-ray | 2.05 Å | A/B=458-768 |
| 3OJM | X-ray | 2.1 Å | B=140-368 |
| 3RI1 | X-ray | 2.1 Å | A/B=458-768 |
| 1EV2 | X-ray | 2.2 Å | E/F/G/H=147-366 |
| 2PVY | X-ray | 2.2 Å | A/B/C/D=458-768 |
| 3DAR | X-ray | 2.2 Å | A/B=146-249 |
| 3OJ2 | X-ray | 2.2 Å | C/D=140-368 |
| 9U7E | X-ray | 2.2 Å | A/B=465-768 |
| 7KIA | X-ray | 2.22 Å | A/B=461-768 |
Showing 20 of 63 experimental structures (best resolution first).
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