Q13651: Interleukin-10 receptor subunit alpha (IL10RA)

Interleukin-10 receptor subunit alpha (IL10RA) is a 578-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13651.

Gene
IL10RA
Organism
Homo sapiens
Length
578 residues
Mean pLDDT
62.0
Model
AF-Q13651-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 62.0 (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 accurate33%
70 to 90Confident: backbone generally right9%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions54%

What pLDDT means and how to read it

Function

Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well (PubMed:16982608). In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively (PubMed:12133952). These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3. Once phosphorylated,…

Subunit structure

Interacts with IL10 (PubMed:15837194, PubMed:16982608). Interacts with IL10RB (PubMed:16982608). Interacts (via its cytoplasmic domain) with JAK1 (via N-terminus) (PubMed:12133952). Interacts with BTRC; this interaction leads to IL10RA ubiquitination and subsequent degradation (PubMed:22087322). Interacts with STAT3 (By similarity)

Subcellular location

Cell membrane, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1Y6KX-ray2.52 ÅR=22-235
5IXIX-ray2.57 ÅB=264-303
1LQSX-ray2.7 ÅR/S=22-235
1Y6NX-ray2.7 ÅR=22-235
1Y6MX-ray2.8 ÅR=22-235
1J7VX-ray2.9 ÅR=22-235
6X93EM3.5 ÅB/E=22-235

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