Fibroblast growth factor 2 (FGF2) is a 288-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P09038.
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The mean pLDDT of this model is 70.3 (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 | 43% |
| 70 to 90 | Confident: backbone generally right | 1% |
| 50 to 70 | Low: treat with caution | 26% |
| Below 50 | Very low: often disordered regions | 30% |
What pLDDT means and how to read it
Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:8663044). Also acts as an integrin ligand which is required for FGF2 signaling (PubMed:28302677). Binds to integrin ITGAV:ITGB3 (PubMed:28302677). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (PubMed:28302677, PubMed:8663044). Functions as a potent mitogen in vitro (PubMed:1721615, PubMed:3732516, PubMed:3964259). Can induce angiogenesis (PubMed:23469107, PubMed:28302677). Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation (PubMed:29501879)
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. Interacts with CSPG4, FGFBP1 and TEC. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP3 (PubMed:18669637). Interacts with integrin ITGAV:ITGB3; the interaction is…
Secreted, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8OM6 | X-ray | 1.31 Å | A=134-288 |
| 8HU7 | X-ray | 1.4 Å | A=142-288 |
| 8HUE | X-ray | 1.48 Å | A/B/C=142-288 |
| 4OEE | X-ray | 1.5 Å | A=134-288 |
| 1BFG | X-ray | 1.6 Å | A=143-288 |
| 4FGF | X-ray | 1.6 Å | A=143-288 |
| 4OEG | X-ray | 1.6 Å | A=134-288 |
| 2FGF | X-ray | 1.77 Å | A=143-288 |
| 4OEF | X-ray | 1.8 Å | A=134-288 |
| 1BAS | X-ray | 1.9 Å | A=135-288 |
| 1BFB | X-ray | 1.9 Å | A=142-288 |
| 5X1O | X-ray | 1.9 Å | A/B=143-288 |
| 1BFF | X-ray | 2.0 Å | A=160-288 |
| 1BFC | X-ray | 2.2 Å | A=142-288 |
| 1EV2 | X-ray | 2.2 Å | A/B/C/D=157-288 |
| 1FGA | X-ray | 2.2 Å | A=143-288 |
| 1IIL | X-ray | 2.3 Å | A/B/C/D=134-288 |
| 2BFH | X-ray | 2.5 Å | A=161-288 |
| 6L4O | X-ray | 2.6 Å | B=135-288 |
| 1II4 | X-ray | 2.7 Å | A/B/C/D=134-288 |
Showing 20 of 25 experimental structures (best resolution first).
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