P29459: Interleukin-12 subunit alpha (IL12A)

Interleukin-12 subunit alpha (IL12A) is a 219-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P29459.

Gene
IL12A
Organism
Homo sapiens
Length
219 residues
Mean pLDDT
79.0
Model
AF-P29459-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.0 (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 right21%
50 to 70Low: treat with caution22%
Below 50Very low: often disordered regions11%

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 (PubMed:8605935, PubMed:8943050). 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:1673147, PubMed:1674604, PubMed:8605935). Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits…

Subunit structure

Heterodimer with IL12B; disulfide-linked (PubMed:10899108, PubMed:1674604). This heterodimer is known as interleukin IL-12 (PubMed:1674604). Heterodimer with EBI3/IL27B; not disulfide-linked (PubMed:9342359). This heterodimer is known as interleukin IL-35 (PubMed:9342359). Interacts with NBR1; this interaction promotes IL-12 secretion (By similarity)

Subcellular location

Secreted

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1F45X-ray2.8 ÅB=23-219
3HMXX-ray3.0 ÅB=23-219
8YI7EM3.57 ÅA=19-219
8XRPEM3.75 ÅA/E/I/M=19-219

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