O76064: E3 ubiquitin-protein ligase RNF8 (RNF8)

E3 ubiquitin-protein ligase RNF8 (RNF8) is a 485-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O76064.

Gene
RNF8
Organism
Homo sapiens
Length
485 residues
Mean pLDDT
75.4
Model
AF-O76064-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.4 (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 right31%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions23%

What pLDDT means and how to read it

Function

E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF) (PubMed:18001824, PubMed:18006705). Also controls the recruitment of UIMC1-BRCC3…

Subunit structure

Homodimer. Forms a E2-E3 ubiquitin ligase complex composed of the RNF8 homodimer and a E2 heterodimer of UBE2N and UBE2V2. Interacts with class III E2s, including UBE2E1, UBE2E2, and UBE2E3 and with UBE2N. Interacts with RXRA. Interacts (via FHA domain) with ATM-phosphorylated MDC1. Interacts (via FHA domain) with 'Thr-4827' phosphorylated HERC2 (via C-terminus). Interacts with PIWIL1; leading…

Subcellular location

Nucleus, Cytoplasm, Midbody, Chromosome, telomere

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2PIEX-ray1.35 ÅA=13-146
4AYCX-ray1.9 ÅA/B=351-485
4ORHX-ray4.8 ÅC/G/H/K/L=345-485
4WHVX-ray8.3 ÅC/D/I/J=345-485
2CSWNMRA=8-139

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