Ubiquitin-conjugating enzyme E2 D2 (UBE2D2) is a 147-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62837.
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The mean pLDDT of this model is 96.5 (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 | 97% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 0% |
| Below 50 | Very low: often disordered regions | 0% |
What pLDDT means and how to read it
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (PubMed:10329681, PubMed:18042044, PubMed:18703417, PubMed:20061386, PubMed:20403326, PubMed:20525694, PubMed:26475854, PubMed:28322253). Catalyzes 'Lys-48'-linked polyubiquitination (PubMed:10329681, PubMed:18042044, PubMed:18359941, PubMed:18703417, PubMed:20061386, PubMed:20403326, PubMed:20525694, PubMed:26475854). Mediates the selective degradation of short-lived and abnormal proteins (PubMed:10329681, PubMed:18042044, PubMed:18359941, PubMed:18703417, PubMed:20061386, PubMed:20403326, PubMed:20525694, PubMed:26475854). Functions in the E6/E6-AP-induced ubiquitination of p53/TP53…
Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Interacts with CNOT4 (via RING domain). Interacts with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with PDZRN3. Interacts with PPP1R11 (By similarity). Interacts with E3 ubiquitin-protein ligase PHF7; the interaction inhibits cleavage of PHF7 and promotes association of the complex with the nucleosome core…
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9GLS | X-ray | 1.25 Å | AAA=1-147 |
| 2ESK | X-ray | 1.36 Å | A=1-147 |
| 6SQO | X-ray | 1.41 Å | B/E=2-147 |
| 2ESQ | X-ray | 1.44 Å | A=1-147 |
| 2ESO | X-ray | 1.5 Å | A=1-147 |
| 2ESP | X-ray | 1.52 Å | A=1-147 |
| 4V3L | X-ray | 1.53 Å | A=2-147 |
| 7AI0 | X-ray | 1.56 Å | BBB/EEE=1-147 |
| 5D1M | X-ray | 1.58 Å | A=1-147 |
| 3L1Y | X-ray | 1.6 Å | A=1-147 |
| 5D1L | X-ray | 1.62 Å | A=1-147 |
| 6HPR | X-ray | 1.7 Å | C=1-147 |
| 8GBQ | X-ray | 1.74 Å | A=1-147 |
| 5D1K | X-ray | 1.78 Å | A=1-147 |
| 3TGD | X-ray | 1.8 Å | A=1-147 |
| 5ULF | X-ray | 1.8 Å | A/C=1-147 |
| 6W7Z | X-ray | 1.8 Å | A=1-147 |
| 7BOL | X-ray | 1.8 Å | A=1-147 |
| 6SQS | X-ray | 1.83 Å | B/E=2-147 |
| 9YEA | X-ray | 1.83 Å | A=1-147 |
Showing 20 of 61 experimental structures (best resolution first).
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