Macrophage colony-stimulating factor 1 receptor (CSF1R) is a 972-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07333.
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The mean pLDDT of this model is 77.8 (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 | 47% |
| 70 to 90 | Confident: backbone generally right | 28% |
| 50 to 70 | Low: treat with caution | 6% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
Tyrosine-protein kinase that acts as a cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development…
Interacts with INPPL1/SHIP2 and THOC5 (By similarity). Monomer. Homodimer. Interacts with CSF1 and IL34. Interaction with dimeric CSF1 or IL34 leads to receptor homodimerization. Interacts (tyrosine phosphorylated) with PLCG2 (via SH2 domain). Interacts (tyrosine phosphorylated) with PIK3R1 (via SH2 domain). Interacts (tyrosine phosphorylated) with FYN, YES1 and SRC (via SH2 domain). Interacts…
Cell membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8JOT | X-ray | 1.69 Å | A=542-919 |
| 6T2W | X-ray | 1.7 Å | A=542-919 |
| 2I1M | X-ray | 1.8 Å | A=538-922 |
| 6IG8 | X-ray | 1.8 Å | A=550-919 |
| 2I0Y | X-ray | 1.9 Å | A=538-922 |
| 8CGC | X-ray | 1.93 Å | A=542-919 |
| 3DPK | X-ray | 1.95 Å | A=538-678, A=753-922 |
| 3BEA | X-ray | 2.02 Å | A=538-678, A=753-922 |
| 3KRJ | X-ray | 2.1 Å | A=538-678, A=753-922 |
| 6N33 | X-ray | 2.25 Å | A=542-919 |
| 8W1L | X-ray | 2.26 Å | A=538-922 |
| 3KRL | X-ray | 2.4 Å | A=538-678, A=753-922 |
| 3LCD | X-ray | 2.5 Å | A=538-922 |
| 4LIQ | X-ray | 2.6 Å | E=2-512 |
| 6WXJ | X-ray | 2.62 Å | A=538-678, A=753-922 |
| 2OGV | X-ray | 2.7 Å | A=543-918 |
| 7TNH | X-ray | 2.7 Å | A=550-678, A=753-922 |
| 4R7I | X-ray | 2.75 Å | A=542-919 |
| 2I0V | X-ray | 2.8 Å | A=538-922 |
| 4R7H | X-ray | 2.8 Å | A=542-919 |
Showing 20 of 26 experimental structures (best resolution first).
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