E3 ubiquitin-protein ligase RNF168 (RNF168) is a 571-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q8IYW5.
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The mean pLDDT of this model is 61.1 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 29% |
| 70 to 90 | Confident: backbone generally right | 8% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 52% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading…
Monomer. Interacts with UBE2N/UBC13
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 5XIS | X-ray | 1.78 Å | A/D=110-188 |
| 5XIU | X-ray | 1.8 Å | A=419-462 |
| 8UQA | X-ray | 2.05 Å | K=1-94 |
| 3L11 | X-ray | 2.12 Å | A=1-113 |
| 5XIT | X-ray | 2.25 Å | A/E=113-188 |
| 8UQ9 | X-ray | 2.3 Å | A/a=1-94 |
| 8UQ8 | X-ray | 2.34 Å | A/a=1-94 |
| 8UQB | X-ray | 2.48 Å | A=1-94 |
| 5YDK | X-ray | 2.5 Å | A/F/G/L=113-194 |
| 4GB0 | X-ray | 2.6 Å | A=1-111 |
| 8UQC | X-ray | 2.61 Å | A=1-94 |
| 8SMX | EM | 3.2 Å | K=1-93 |
| 8SMY | EM | 3.2 Å | K=1-93 |
| 8SMZ | EM | 3.2 Å | K=1-93 |
| 8SN0 | EM | 3.2 Å | K=1-93 |
| 8UPF | EM | 3.2 Å | K=1-94 |
| 8X7I | EM | 3.27 Å | L=1-113 |
| 8X7K | EM | 3.27 Å | L=1-113 |
| 8SMW | EM | 3.3 Å | K=1-93 |
| 8SN1 | EM | 3.3 Å | K=1-93 |
Showing 20 of 39 experimental structures (best resolution first).
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