Q14653: Interferon regulatory factor 3 (IRF3)

Interferon regulatory factor 3 (IRF3) is a 427-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q14653.

Gene
IRF3
Organism
Homo sapiens
Length
427 residues
Mean pLDDT
80.3
Model
AF-Q14653-F1 v6
Model created
1 Aug 2025
PDB structures
18

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Model confidence (pLDDT)

The mean pLDDT of this model is 80.3 (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 accurate54%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22394562, PubMed:24049179, PubMed:25636800, PubMed:27302953, PubMed:31340999, PubMed:36603579, PubMed:8524823, PubMed:39362857). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:11846977, PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:32972995, PubMed:36603579, PubMed:8524823). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA)…

Subunit structure

Monomer (PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:36603579). Homodimer; phosphorylation-induced (PubMed:22394562, PubMed:25636800, PubMed:26347139, PubMed:36603579). Interacts (when phosphorylated) with CREBBP (PubMed:16154084, PubMed:27302953). Interacts with MAVS (via phosphorylated pLxIS motif) (PubMed:16153868, PubMed:25636800, PubMed:27302953). Interacts with TICAM1 (via…

Subcellular location

Cytoplasm, Nucleus, Mitochondrion

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6SJAX-ray1.5 ÅA=137-148
5JELX-ray1.6 ÅA=189-427
7JFLX-ray1.68 ÅA/B=189-398
5JEOX-ray1.72 ÅA=189-427
6SIVX-ray1.75 ÅA=137-148
3A77X-ray1.8 ÅA/B/C/D=189-427
5JEJX-ray2.0 ÅA/B=189-427
1QWTX-ray2.1 ÅA/B=173-427
1J2FX-ray2.3 ÅA/B=175-427
3QU6X-ray2.3 ÅA/B/C=1-113
2PI0X-ray2.31 ÅA/B/C/D=1-113
1ZOQX-ray2.37 ÅA/B=196-386
5JEKX-ray2.4 ÅA/B=189-427
5JEMX-ray2.5 ÅA/B/E/G=189-398
2O61X-ray2.8 ÅA=9-111
5JERX-ray2.91 ÅA/C/E/G=189-427
1T2KX-ray3.0 ÅA/B=1-112
2O6GX-ray3.1 ÅE/F/G/H=1-123

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