Q92878: DNA repair protein RAD50 (RAD50)

DNA repair protein RAD50 (RAD50) is a 1312-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q92878.

Gene
RAD50
Organism
Homo sapiens
Length
1312 residues
Mean pLDDT
82.8
Model
AF-Q92878-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.8 (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 accurate15%
70 to 90Confident: backbone generally right78%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions1%

What pLDDT means and how to read it

Function

Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28134932, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:15064416, PubMed:21757780, PubMed:27889449, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a…

Subunit structure

Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single NBN (PubMed:10839544, PubMed:26215093, PubMed:28867292, PubMed:36577401, PubMed:8756642, PubMed:9590181, PubMed:9705271). The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:36577401). As part of the MRN complex, interacts with MCM8…

Subcellular location

Nucleus, Chromosome, telomere, Chromosome

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5GOXX-ray2.4 ÅA/B=585-766
9Q9KEM2.59 ÅA/B=1-1312
9Q9JEM2.71 ÅA/B=1-1312
9Q9IEM2.79 ÅA/B=1-1312
9Q9MEM2.81 ÅA/B=1-1312
9Q9HEM3.11 ÅA/B=1-1312

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