P48551: Interferon alpha/beta receptor 2 (IFNAR2)

Interferon alpha/beta receptor 2 (IFNAR2) is a 515-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P48551.

Gene
IFNAR2
Organism
Homo sapiens
Length
515 residues
Mean pLDDT
64.4
Model
AF-P48551-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate27%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution20%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:10049744, PubMed:10556041, PubMed:21854986, PubMed:26424569, PubMed:28165510, PubMed:32972995, PubMed:7665574, PubMed:7759950, PubMed:8181059, PubMed:8798579, PubMed:8969169). 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:17517919, PubMed:21854986, PubMed:26424569, PubMed:28165510, PubMed:32972995, PubMed:7665574, PubMed:7759950, PubMed:8181059, PubMed:8798579,…

Subunit structure

Heterodimer with IFNAR1; forming the receptor for type I interferon (PubMed:10049744, PubMed:21854986, PubMed:24075985, PubMed:7665574, PubMed:8181059). Interacts with JAK1 (PubMed:7759950, PubMed:8181059). Interacts with the transcriptional factors STAT1 and STAT2 (PubMed:28165510, PubMed:9121453). Interacts with USP18; indirectly via STAT2, it negatively regulates the assembly of the ternary…

Subcellular location

Cell membrane, Secreted

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3S9DX-ray2.0 ÅB/D=37-232
3S8WX-ray2.6 ÅA/B/C=131-232
3SE4X-ray3.5 ÅC=34-232
3SE3X-ray4.0 ÅC=34-232
1N6UNMRA=28-237
1N6VNMRA=28-237
2HYMNMRA=28-237
2KZ1NMRB=28-237
2LAGNMRB=28-237

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