Interleukin-6 receptor subunit alpha (IL6R) is a 468-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P08887.
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The mean pLDDT of this model is 77.9 (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 | 54% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 24% |
What pLDDT means and how to read it
Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal (PubMed:28265003). Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis (PubMed:30995492, PubMed:31235509). The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R…
Component of a hexamer of two molecules each of IL6, IL6R and IL6ST; first binds to IL6 to associate with the signaling subunit IL6ST (PubMed:12829785, PubMed:28265003). Interacts (via N-terminal ectodomain) with SORL1; this interaction may affect IL6-binding to IL6R, hence decrease IL6 'classic-signaling' (PubMed:28265003)
Cell membrane, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1N26 | X-ray | 2.4 Å | A=20-344 |
| 5FUC | X-ray | 2.7 Å | C/D=111-322 |
| 7DC8 | X-ray | 2.76 Å | C/F=111-320 |
| 8QY5 | EM | 3.1 Å | C/F=1-468 |
| 8QY6 | EM | 3.16 Å | C/F=1-468 |
| 8IOW | EM | 3.2 Å | D2/I=1-355 |
| 8D82 | EM | 3.22 Å | C/G=20-331 |
| 8J6F | EM | 3.3 Å | B=122-131, I=1-355 |
| 1P9M | X-ray | 3.65 Å | C=115-315 |
| 2ARW | NMR | A=212-336 |
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