Q61730: Interleukin-1 receptor accessory protein (Il1rap)

Interleukin-1 receptor accessory protein (Il1rap) is a 570-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q61730.

Gene
Il1rap
Organism
Mus musculus
Length
570 residues
Mean pLDDT
85.8
Model
AF-Q61730-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.8 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate53%
70 to 90Confident: backbone generally right38%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with…

Subunit structure

The interleukin-36 receptor complex is a heterodimer of IL1RL2 and IL1RAP; the association is inhibited by IL36RN. The interleukin-1 receptor complex is a heterodimer of IL1R1 and IL1RAP. Associates with IL1R2 to form a non-signaling interleukin-1 receptor complex. Interacts with IL-33-bound IL1RL1 to form the minimal interleukin-33 signaling complex with a 1:1:1 stoichiometry. Interacts with…

Subcellular location

Cell membrane, Secreted

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5VI4X-ray2.79 ÅC/F=21-350
4YFDX-ray3.25 ÅB=21-351

More AlphaFold highlights

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