Interferon regulatory factor 4 (IRF4) is a 451-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15306.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 71.6 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 46% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 34% |
What pLDDT means and how to read it
Transcriptional activator. Binds to the interferon-stimulated response element (ISRE) of the MHC class I promoter. Binds the immunoglobulin lambda light chain enhancer, together with PU.1. Probably plays a role in ISRE-targeted signal transduction mechanisms specific to lymphoid cells. Involved in CD8(+) dendritic cell differentiation by forming a complex with the BATF-JUNB heterodimer in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 and activation of genes
Interacts with the BATF-JUNB heterodimer. Interacts with BATF (via bZIP domain); the interaction is direct (By similarity). Interacts with SPIB (PubMed:10196196). Interacts with DEF6 (PubMed:12651066). Directly interacts with NLRP3 in the nucleus of Th2 cells; this interaction enhances IRF4 ability to bind to the IL4 promoter and is required for optimal IRF4-dependent IL4 transcription (By…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6TD4 | X-ray | 1.71 Å | A=20-132 |
| 9VEH | X-ray | 2.0 Å | A=205-227 |
| 9TOY | X-ray | 2.1 Å | A/B/D/F=20-139 |
| 9VE3 | X-ray | 2.1 Å | A=205-227 |
| 9VE7 | X-ray | 2.15 Å | A=205-227 |
| 7OOT | X-ray | 2.25 Å | A/B=20-139 |
| 7OGS | X-ray | 2.37 Å | A/B/E/F=20-139 |
| 7RH2 | X-ray | 2.47 Å | A/B/G/H=21-129 |
| 9VE4 | X-ray | 2.55 Å | A=205-227 |
| 7O56 | X-ray | 2.6 Å | A/B/C=20-139 |
| 9VE6 | X-ray | 2.8 Å | A=205-227 |
| 9VE8 | X-ray | 2.85 Å | A=205-227 |
| 7JM4 | X-ray | 2.95 Å | A/B/G/H=21-129 |
| 21IK | X-ray | 2.99 Å | A=205-227 |
| 9VE5 | X-ray | 3.2 Å | A=205-227 |
| 21IE | X-ray | 3.24 Å | A=205-226 |
| 21IP | X-ray | 3.3 Å | A=205-227 |
| 9VEA | X-ray | 3.6 Å | A=205-227 |
| 2DLL | NMR | A=23-130 |
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