RAF proto-oncogene serine/threonine-protein kinase (RAF1) is a 648-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04049.
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The mean pLDDT of this model is 67.5 (low 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 | 30% |
| 70 to 90 | Confident: backbone generally right | 27% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 36% |
What pLDDT means and how to read it
Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death…
Monomer. Homodimer. Heterodimerizes with BRAF and this heterodimer possesses a highly increased kinase activity compared to the respective homodimers or monomers (PubMed:16508002). Heterodimerization is mitogen-regulated and enhanced by 14-3-3 proteins (PubMed:16508002). MAPK1/ERK2 activation can induce a negative feedback that promotes the dissociation of the heterodimer (PubMed:16508002).…
Cytoplasm, Cell membrane, Mitochondrion, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3IQU | X-ray | 1.05 Å | P=255-260 |
| 3IQJ | X-ray | 1.15 Å | P=255-264 |
| 3IQV | X-ray | 1.2 Å | P=255-260 |
| 6VJJ | X-ray | 1.4 Å | B=52-131 |
| 8ATS | X-ray | 1.4 Å | P=255-263 |
| 9EW1 | X-ray | 1.4 Å | P=255-263 |
| 9EW3 | X-ray | 1.4 Å | P=255-263 |
| 8AV0 | X-ray | 1.5 Å | P=256-264 |
| 9EW5 | X-ray | 1.5 Å | C/F=255-265 |
| 9S2J | X-ray | 1.5 Å | P=255-265 |
| 9S2P | X-ray | 1.5 Å | P=255-265 |
| 8A68 | X-ray | 1.6 Å | B=255-263 |
| 8A6F | X-ray | 1.6 Å | P=255-264 |
| 8A6H | X-ray | 1.6 Å | P=255-264 |
| 9EW4 | X-ray | 1.6 Å | P=255-263 |
| 8JNB | X-ray | 1.62 Å | B=50-98, B=115-119, B=122-128, B=130-141 |
| 8T74 | X-ray | 1.65 Å | B=52-131 |
| 9S2I | X-ray | 1.67 Å | P=255-265 |
| 4IEA | X-ray | 1.7 Å | P=618-625 |
| 8ATR | X-ray | 1.7 Å | P=255-263 |
Showing 20 of 75 experimental structures (best resolution first).
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