DCN1-like protein 1 (DCUN1D1) is a 259-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q96GG9.
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The mean pLDDT of this model is 92.1 (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 | 82% |
| 70 to 90 | Confident: backbone generally right | 12% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 1% |
What pLDDT means and how to read it
Part of an E3 ubiquitin ligase complex for neddylation (PubMed:18826954). Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes (PubMed:19617556, PubMed:23201271, PubMed:23401859, PubMed:26906416). Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity (PubMed:25349211, PubMed:28581483). Also acts as…
Part of an E3 complex for neddylation composed of cullins, RBX1, UBE2M and CAND1 (PubMed:18826954). Interacts (via the DCUN1 domain) with the unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these interactions promote the cullin neddylation and the identity of the cullin dictates the affinity of the interaction (PubMed:18826954, PubMed:19617556, PubMed:23201271,…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6BG3 | X-ray | 1.05 Å | A=62-259 |
| 6BG5 | X-ray | 1.1 Å | A=62-259 |
| 5V86 | X-ray | 1.37 Å | A=62-259 |
| 6P5V | X-ray | 1.4 Å | A=62-259 |
| 3TDU | X-ray | 1.5 Å | A/B=62-259 |
| 7KWA | X-ray | 1.57 Å | A=62-259 |
| 5V88 | X-ray | 1.6 Å | A=62-259 |
| 6P5W | X-ray | 1.69 Å | A=62-259 |
| 3TDZ | X-ray | 2.0 Å | A/B=62-259 |
| 5V83 | X-ray | 2.0 Å | A=62-259 |
| 6XOO | X-ray | 2.06 Å | A=62-259 |
| 6XOP | X-ray | 2.07 Å | A=62-259 |
| 6XOQ | X-ray | 2.07 Å | A=62-259 |
| 6XOM | X-ray | 2.1 Å | A=62-259 |
| 6B5Q | X-ray | 2.16 Å | A/B=58-259 |
| 6XOL | X-ray | 2.39 Å | A=62-259 |
| 5UFI | X-ray | 2.58 Å | A/B/C/D=58-259 |
| 6XON | X-ray | 2.8 Å | A=62-259 |
| 8OR3 | EM | 2.9 Å | F=1-259 |
| 4P5O | X-ray | 3.11 Å | E/F=61-259 |
Showing 20 of 21 experimental structures (best resolution first).
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