Ubiquitin-conjugating enzyme E2 N (UBE2N) is a 152-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61088.
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The mean pLDDT of this model is 95.7 (very high 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 | 95% |
| 70 to 90 | Confident: backbone generally right | 4% |
| 50 to 70 | Low: treat with caution | 1% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked…
Heterodimer with UBE2V2 (PubMed:10089880, PubMed:11473255, PubMed:14562038, PubMed:16307917). Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity (PubMed:16307917). Interacts with RNF8 and RNF168 (PubMed:16215985, PubMed:19203578). Interacts with RNF11 (PubMed:18615712). Interacts with the E3…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4ONL | X-ray | 1.35 Å | B=1-152 |
| 4ONM | X-ray | 1.35 Å | B=1-152 |
| 5YWR | X-ray | 1.47 Å | A=1-152 |
| 4ONN | X-ray | 1.5 Å | B=1-152 |
| 9BIV | X-ray | 1.68 Å | B=1-152 |
| 9LHJ | X-ray | 1.68 Å | A/B=1-152 |
| 4DHI | X-ray | 1.8 Å | D=1-152 |
| 4NR3 | X-ray | 1.8 Å | B=2-150 |
| 1J7D | X-ray | 1.85 Å | B=1-152 |
| 4NRG | X-ray | 1.95 Å | B=1-152 |
| 6ULH | X-ray | 1.97 Å | C=1-152 |
| 4TKP | X-ray | 2.08 Å | A=2-152 |
| 3HCT | X-ray | 2.1 Å | B=1-152 |
| 6P5B | X-ray | 2.1 Å | C=1-152 |
| 9N1F | X-ray | 2.1 Å | B=1-152 |
| 7BBD | X-ray | 2.2 Å | C=1-152 |
| 5AIU | X-ray | 2.21 Å | B/E=1-152 |
| 4IP3 | X-ray | 2.3 Å | B=1-152 |
| 4NRI | X-ray | 2.3 Å | B=3-150 |
| 6UMS | X-ray | 2.34 Å | C=1-152 |
Showing 20 of 44 experimental structures (best resolution first).
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