Fibroblast growth factor 1 (FGF1) is a 155-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P05230.
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The mean pLDDT of this model is 90.7 (very high 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 | 81% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 5% |
What pLDDT means and how to read it
Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and…
Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1. Part of a Cu(2+)-dependent multiprotein aggregate containing FGF1, S100A13 and SYT1. Interacts with SYT1.…
Secreted, Cytoplasm, Cytoplasm, cell cortex, Cytoplasm, cytosol, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1RG8 | X-ray | 1.1 Å | A/B=16-155 |
| 4QC4 | X-ray | 1.49 Å | A/B=16-155 |
| 3BB2 | X-ray | 1.5 Å | A/B=16-155 |
| 4QAL | X-ray | 1.5 Å | A/B=16-155 |
| 4QBV | X-ray | 1.5 Å | A/B=16-155 |
| 4QBC | X-ray | 1.52 Å | A/B=16-155 |
| 3B9U | X-ray | 1.55 Å | A=16-155 |
| 3BAO | X-ray | 1.55 Å | A/B=16-155 |
| 4Q9G | X-ray | 1.55 Å | A/B=16-155 |
| 1P63 | X-ray | 1.6 Å | A/B=16-155 |
| 2HW9 | X-ray | 1.6 Å | A/B=16-155 |
| 2HWM | X-ray | 1.6 Å | A/B=16-155 |
| 3BA7 | X-ray | 1.6 Å | A/B=16-155 |
| 3BAU | X-ray | 1.6 Å | A/B=16-155 |
| 3O3Q | X-ray | 1.6 Å | A/B/C/D=16-155 |
| 3BAV | X-ray | 1.62 Å | A/B=16-155 |
| 1JQZ | X-ray | 1.65 Å | A/B=16-155 |
| 2HWA | X-ray | 1.65 Å | A/B=16-155 |
| 3BAH | X-ray | 1.65 Å | A/B=16-155 |
| 1JT7 | X-ray | 1.7 Å | A/B/C/D=16-155 |
Showing 20 of 96 experimental structures (best resolution first).
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