P17181: Interferon alpha/beta receptor 1 (IFNAR1)

Interferon alpha/beta receptor 1 (IFNAR1) is a 557-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P17181.

Gene
IFNAR1
Organism
Homo sapiens
Length
557 residues
Mean pLDDT
78.0
Model
AF-P17181-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 78.0 (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 accurate46%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions21%

What pLDDT means and how to read it

Function

Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:10049744, PubMed:14532120, PubMed:15337770, PubMed:2153461, PubMed:21854986, PubMed:24075985, PubMed:31270247, PubMed:33252644, PubMed:35442418, PubMed:7813427). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (PubMed:10049744, PubMed:21854986, PubMed:7665574). Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving…

Subunit structure

Heterodimer with IFNAR2; forming the receptor for type I interferon (PubMed:10049744, PubMed:21854986, PubMed:7665574). Interacts with TYK2 (PubMed:15337770, PubMed:24704786, PubMed:7526154). Interacts with STAT1 and STAT2; the interaction requires its phosphorylation at Tyr-466 (PubMed:9121453). Interacts (serine-phosphorylated form) with FBXW11, the substrate recognition component of a SCF…

Subcellular location

Cell membrane, Late endosome, Lysosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3S98X-ray1.9 ÅA=30-332
4PO6X-ray1.99 ÅB=478-507
8Y31X-ray2.68 ÅE/F=1-333
3SE4X-ray3.5 ÅA=28-436
3SE3X-ray4.0 ÅA=28-436

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