Q99708: DNA endonuclease RBBP8 (RBBP8)

DNA endonuclease RBBP8 (RBBP8) is a 897-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99708.

Gene
RBBP8
Organism
Homo sapiens
Length
897 residues
Mean pLDDT
53.0
Model
AF-Q99708-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 53.0 (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 accurate13%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions64%

What pLDDT means and how to read it

Function

Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:31802118). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical…

Subunit structure

Homotetramer; formed by antiparallel association of helical extensions protruding from the N-termini of two parallel coiled-coil dimers (PubMed:15084581, PubMed:25558984, PubMed:30601117, PubMed:34129781). Forms a dumbbell-shaped particle in which polar globular domains are held about 30 nm apart by a central rod (PubMed:30601117). Homotetramerization is required for DNA-end resection and repair…

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
4D2HX-ray1.9 ÅA/B/C/D/E/F/G/H=18-52
1Y98X-ray2.5 ÅB=322-333
7BGFX-ray2.8 ÅA/B=31-152
2L4ZNMRA=641-685

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