Q9NRZ9: Lymphoid-specific helicase (HELLS)

Lymphoid-specific helicase (HELLS) is a 838-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9NRZ9.

Gene
HELLS
Organism
Homo sapiens
Length
838 residues
Mean pLDDT
68.4
Model
AF-Q9NRZ9-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 68.4 (low 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 accurate20%
70 to 90Confident: backbone generally right34%
50 to 70Low: treat with caution23%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements (PubMed:30307408). Also involved in DNA repair by recruiting DNA damage response mediators to double-strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection (PubMed:22946062, PubMed:31802118). During meiosis, it is recruited by PRDM9 to recombination hotspots,…

Subunit structure

Interacts with RBBP8/CtIP; the interaction leads to recruitment of RBBP8/CtIP to sites of DNA breaks (PubMed:31802118). Interacts with PRDM9; the interaction recruits HELLS to meiotic recombination hot spots (PubMed:32001511). Interacts with CDCA7; the interaction brings HELLS to chromatin and recruits DNA methyltransferases to heterochromatin regions (PubMed:30307408)

Subcellular location

Nucleus, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9Z05EM2.86 ÅA/B/C/D/E/F=1-838
9Z04EM2.99 ÅA/B/C/D/E/F=1-838
9Z06EM3.39 ÅA/B/C/D/E/F=1-838
8SKZEM3.5 ÅA=500-553

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