Q96HA7: Tonsoku-like protein (TONSL)

Tonsoku-like protein (TONSL) is a 1378-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96HA7.

Gene
TONSL
Organism
Homo sapiens
Length
1378 residues
Mean pLDDT
75.3
Model
AF-Q96HA7-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.3 (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 accurate43%
70 to 90Confident: backbone generally right30%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions24%

What pLDDT means and how to read it

Function

Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:21113133, PubMed:26527279, PubMed:27338793, PubMed:27797818, PubMed:29478807, PubMed:30773278). The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication (PubMed:21055983, PubMed:21055984, PubMed:21055985). It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex…

Subunit structure

Component of the MMS22L-TONSL complex, a complex at least composed of MMS22L and TONSL/NFKBIL2 (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:21113133, PubMed:27338793). Interacts with the MCM complex, the FACT complex and the RPA complex (PubMed:21055983, PubMed:21055984, PubMed:26527279). Interacts with MCM5; the interaction is direct (PubMed:26527279). Binds histones, with a…

Subcellular location

Nucleus, Chromosome, Cytoplasm

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9WVHX-ray1.96 ÅA/B=933-1011
9WVIX-ray2.19 ÅA/B/C/D=933-1011
5JA4X-ray2.42 ÅD=512-692

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