Q96C10: ATP-dependent RNA helicase DHX58 (DHX58)

ATP-dependent RNA helicase DHX58 (DHX58) is a 678-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96C10.

Gene
DHX58
Organism
Homo sapiens
Length
678 residues
Mean pLDDT
91.0
Model
AF-Q96C10-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 91.0 (very high 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 accurate72%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Acts as a regulator of RIGI and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to RIGI and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on RIG-I signaling may involve the following mechanisms: competition with RIGI for binding to the viral RNA, binding to RIGI and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to…

Subunit structure

Monomer in the absence of dsRNA. Homodimer in the presence of dsRNA. Interacts with RIGI (via CARD domain), MAVS/IPS1 and DDX60. Found in a complex with RIGI and IFIH1/MDA5. Interacts with ANKRD17. Directly interacts with ATG5 and ATG12, either as ATG5 and ATG12 monomers or as ATG12-ATG5 conjugates (PubMed:17709747)

Subcellular location

Cytoplasm

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3EQTX-ray2.0 ÅA/B=541-678
2W4RX-ray2.6 ÅA/B/C/D=537-678
9LOVEM3.07 ÅA=1-678
9LOUEM3.36 ÅA=1-678
2RQANMRA=546-678

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