O60934: Nibrin (NBN)

Nibrin (NBN) is a 754-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60934.

Gene
NBN
Organism
Homo sapiens
Length
754 residues
Mean pLDDT
63.1
Model
AF-O60934-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 63.1 (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 accurate30%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution11%
Below 50Very low: often disordered regions45%

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:10888888, PubMed:15616588, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:23115235, PubMed:28216226, PubMed:28867292, 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:19759395, PubMed:28867292, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and…

Subunit structure

Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single NBN (PubMed:11238951, PubMed:26215093, PubMed:28867292, PubMed:36577401, 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 MCM9; the…

Subcellular location

Nucleus, Chromosome, Nucleus, PML body, Chromosome, telomere

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7SIDEM2.53 ÅB/D=727-754
9Q9JEM2.71 ÅF=1-754
9Q9IEM2.79 ÅF=1-754
9Q9MEM2.81 ÅF=1-754
5WQDX-ray3.0 ÅH/I/J/K/L/M/N=423-438
9ULOEM3.91 ÅC=1-754
8BAHEM4.13 ÅC=1-754

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