O43143: ATP-dependent RNA helicase DHX15 (DHX15)

ATP-dependent RNA helicase DHX15 (DHX15) is a 795-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43143.

Gene
DHX15
Organism
Homo sapiens
Length
795 residues
Mean pLDDT
85.9
Model
AF-O43143-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 85.9 (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 accurate66%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions9%

What pLDDT means and how to read it

Function

RNA helicase involved in mRNA processing and antiviral innate immunity (PubMed:19103666, PubMed:19432882, PubMed:24782566, PubMed:24990078, PubMed:32179686, PubMed:34161762). Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (PubMed:19103666). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (PubMed:19103666). Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome (PubMed:24782566, PubMed:24990078, PubMed:34161762). Acts as an…

Subunit structure

Component of the U11/U12 snRNPs that are part of the U12-type spliceosome (PubMed:15146077). Identified in the Intron Large spliceosome complex (IL, also named intron lariat spliceosome), a post-mRNA release spliceosomal complex containing the excised intron, U2, U5 and U6 snRNPs, and splicing factors; the association may be transient (PubMed:19103666, PubMed:30728453). The IL complex exists in…

Subcellular location

Nucleus, Nucleus, nucleolus

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8EJMX-ray1.8 ÅA=113-795
6SH6X-ray1.85 ÅA=113-795
5XDRX-ray2.0 ÅA=110-795
6SH7X-ray2.21 ÅA=113-795
6ID1EM2.86 ÅV=1-795
8RO2EM3.5 ÅDX=1-795

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