Q9BYX4: Interferon-induced helicase C domain-containing protein 1 (IFIH1)

Interferon-induced helicase C domain-containing protein 1 (IFIH1) is a 1025-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9BYX4.

Gene
IFIH1
Organism
Homo sapiens
Length
1025 residues
Mean pLDDT
79.4
Model
AF-Q9BYX4-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 79.4 (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 accurate44%
70 to 90Confident: backbone generally right38%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions14%

What pLDDT means and how to read it

Function

Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and pro-inflammatory cytokines (PubMed:28594402, PubMed:32169843, PubMed:33727702). Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length) (PubMed:22160685). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of…

Subunit structure

Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA (PubMed:33727702). Interacts with MAVS/IPS1. Interacts (via the CARD domains) with TKFC, the interaction is inhibited by viral infection (PubMed:17600090). Interacts with PCBP2. Interacts with NLRC5. Interacts with PIAS2-beta. Interacts with…

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
3GA3X-ray1.45 ÅA=893-1017
3B6EX-ray1.6 ÅA=277-490
9LOVEM3.07 ÅB/C=287-1025
7DNIEM3.2 ÅA/B/C/D=1-208
7DNJEM3.3 ÅA/B/C/D=1-208
4GL2X-ray3.56 ÅA/B=306-1017
7JL0EM4.3 ÅA=287-1025
7JL2EM4.3 ÅA/C/E=287-1025
2RQBNMRA=896-1025

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