P43431: Interleukin-12 subunit alpha (Il12a)

Interleukin-12 subunit alpha (Il12a) is a 215-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P43431.

Gene
Il12a
Organism
Mus musculus
Length
215 residues
Mean pLDDT
79.8
Model
AF-P43431-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.8 (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 accurate40%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution16%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

Heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine. IL-12 is primarily produced by professional antigen-presenting cells (APCs) such as B-cells and dendritic cells (DCs) as well as macrophages and granulocytes and regulates T-cell and natural killer-cell responses, induces the production of interferon-gamma (IFN-gamma), favors the differentiation of T-helper 1 (Th1) cells and is an important link between innate resistance and adaptive immunity (PubMed:8766560). Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits. Binding to the receptor results in the rapid tyrosine phosphorylation of a…

Subunit structure

Heterodimer with IL12B; disulfide-linked (PubMed:1350290). This heterodimer is known as interleukin IL-12 (PubMed:1350290). Heterodimer with EBI3/IL27B; not disulfide-linked (By similarity). This heterodimer is known as interleukin IL-35 (By similarity). Interacts with NBR1; this interaction promotes IL-12 secretion (PubMed:34374750)

Subcellular location

Secreted

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8CR6X-ray2.85 ÅB=1-215
8PB1EM3.5 ÅA=23-215
8ODZEM3.6 ÅA=23-215
8OE0EM4.6 ÅA=23-215

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