Interleukin-1 receptor-associated kinase 4 (IRAK4) is a 460-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NWZ3.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 83.9 (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 | 61% |
| 70 to 90 | Confident: backbone generally right | 23% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways (PubMed:17878374). Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation to form the Myddosome together with IRAK2. Phosphorylates initially IRAK1, thus stimulating the kinase activity and intensive autophosphorylation of IRAK1. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the…
Associates with MYD88 and IRAK2 to form a ternary complex called the Myddosome (PubMed:16951688, PubMed:24316379). Once phosphorylated, IRAK4 dissociates from the receptor complex and then associates with the TNF receptor-associated factor 6 (TRAF6), IRAK1, and PELI1; this intermediate complex is required for subsequent NF-kappa-B activation (PubMed:11960013, PubMed:12496252, PubMed:16951688).…
Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6EGE | X-ray | 1.4 Å | A/D=164-460 |
| 9NA5 | X-ray | 1.73 Å | A/B/C/D=160-460 |
| 6UYA | X-ray | 1.74 Å | A/B/C/D=160-460 |
| 8W3X | X-ray | 1.76 Å | A/B/C/D=154-460 |
| 6O95 | X-ray | 1.77 Å | A/B/C/D=160-460 |
| 6O8U | X-ray | 1.8 Å | A/B/C/D=160-460 |
| 8UCC | X-ray | 1.8 Å | A/B=154-460 |
| 5UIT | X-ray | 1.84 Å | A/B=154-460 |
| 8UCB | X-ray | 1.85 Å | A/B/C/D=154-460 |
| 9R9K | X-ray | 1.87 Å | A/B/C/D=154-460 |
| 9R9G | X-ray | 1.88 Å | A/B/C/D=154-460 |
| 8SCE | X-ray | 1.89 Å | A/B/D/E=160-460 |
| 9PSS | X-ray | 1.93 Å | A/B=160-460 |
| 8TVN | X-ray | 1.95 Å | A/B/C/D=154-460 |
| 6O94 | X-ray | 1.98 Å | A/B/C/D=160-460 |
| 8W3W | X-ray | 1.98 Å | A/B/C/D=154-460 |
| 6THX | X-ray | 1.99 Å | A/B=154-460 |
| 9NA2 | X-ray | 1.99 Å | A/B=160-460 |
| 2NRU | X-ray | 2.0 Å | A/B/C/D=154-460 |
| 2OIB | X-ray | 2.0 Å | A/B/C/D=160-460 |
Showing 20 of 96 experimental structures (best resolution first).
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.