Interleukin-15 receptor subunit alpha (IL15RA) is a 267-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13261.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 64.4 (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 | 25% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 23% |
| Below 50 | Very low: often disordered regions | 40% |
What pLDDT means and how to read it
High-affinity receptor for interleukin-15 (PubMed:8530383). Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (By similarity). In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (PubMed:15123770). In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner (PubMed:15123770). Expression of different isoforms may alter or interfere with signal transduction (PubMed:10480910)
The interleukin-15 receptor IL15R is a heterotrimer of IL15RA, IL2RB and IL2RG. IL15RA also self-associates (PubMed:17643103). Interacts with SYK (PubMed:15123770)
Membrane, Nucleus membrane, Cell surface, Endoplasmic reticulum membrane, Golgi apparatus membrane, Cytoplasmic vesicle membrane, Secreted, extracellular space
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2Z3Q | X-ray | 1.85 Å | B/D=31-132 |
| 2Z3R | X-ray | 2.0 Å | B/D/F/H/J/L/N/P=31-132 |
| 4GS7 | X-ray | 2.35 Å | D=30-97 |
| 2ERS | NMR | A=31-96 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.