Ubiquitin-protein ligase E3A (UBE3A) is a 875-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q05086.
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The mean pLDDT of this model is 80.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 51% |
| 70 to 90 | Confident: backbone generally right | 30% |
| 50 to 70 | Low: treat with caution | 4% |
| Below 50 | Very low: often disordered regions | 14% |
What pLDDT means and how to read it
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates (PubMed:10373495, PubMed:16772533, PubMed:19204938, PubMed:19233847, PubMed:19325566, PubMed:19591933, PubMed:22645313, PubMed:24273172, PubMed:24728990, PubMed:30020076). Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B (PubMed:10373495, PubMed:19204938, PubMed:19325566, PubMed:19591933, PubMed:22645313, PubMed:24728990, PubMed:30020076). Additionally, may function as a…
The active form is probably a homotrimer. Binds UBQLN1 and UBQLN2. Interacts with the 26S proteasome. Interacts with BPY2. Interacts with HIF1AN, MAPK6 and NEURL4; interaction with MAPK6 may be mediated by NEURL4. Interacts with the proteasomal subunit PSMD4. Interacts with ESR1 and WBP2 (PubMed:16772533, PubMed:21642474). Interacts with BMAL1 (PubMed:24728990). Interacts with ARC (By similarity)
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6TGK | X-ray | 1.3 Å | C=765-869 |
| 6SJV | X-ray | 2.03 Å | A=171-259, A=403-417 |
| 4XR8 | X-ray | 2.25 Å | A/B=406-417 |
| 7QPB | X-ray | 2.34 Å | A/B/C/D=764-875 |
| 4GIZ | X-ray | 2.55 Å | A/B=400-417 |
| 9L3L | X-ray | 2.59 Å | A=765-872 |
| 1C4Z | X-ray | 2.6 Å | A/B/C=518-875 |
| 8JRN | EM | 2.6 Å | A/C=1-875 |
| 1D5F | X-ray | 2.8 Å | A/B/C=518-875 |
| 6SLM | X-ray | 2.8 Å | A=403-417 |
| 7Q41 | X-ray | 3.01 Å | B/D/F=183-197 |
| 8JRO | EM | 3.01 Å | A/C=1-875 |
| 8GCR | EM | 3.38 Å | R=1-875 |
| 9CHT | EM | 3.54 Å | A=1-875 |
| 8JRP | EM | 3.58 Å | A/C=1-875 |
| 8R1F | EM | 3.67 Å | A=1-875 |
| 8R1G | EM | 3.99 Å | A/D=1-875 |
| 8JRQ | EM | 4.15 Å | A/C=1-875 |
| 8JRR | EM | 4.35 Å | A/C=1-875 |
| 1EQX | NMR | A=401-418 |
Showing 20 of 25 experimental structures (best resolution first).
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