DDB1- and CUL4-associated factor 1 (DCAF1) is a 1507-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9Y4B6.
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The mean pLDDT of this model is 74.9 (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 | 45% |
| 70 to 90 | Confident: backbone generally right | 25% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 25% |
What pLDDT means and how to read it
Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2 (PubMed:23063525). Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex…
Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex. Interacts with DDB1; the interaction is direct. Also forms a ternary complex with DDA1 and DDB1. Interacts with NF2 (via FERM domain). Component of the EDVP complex, a E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and DCAF1 (PubMed:19287380, PubMed:24357321,…
Cytoplasm, Nucleus, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9PLY | X-ray | 1.4 Å | A/B=1077-1390 |
| 9BHS | X-ray | 1.43 Å | A/B=1077-1390 |
| 9Y4Q | X-ray | 1.48 Å | A/B=1077-1390 |
| 8OOD | X-ray | 1.5 Å | A=1039-1401 |
| 9YDG | X-ray | 1.54 Å | A/B=1080-1390 |
| 8F8E | X-ray | 1.55 Å | A/B=1077-1390 |
| 9Y76 | X-ray | 1.56 Å | A/B=1077-1390 |
| 9YV4 | X-ray | 1.6 Å | A/B=1080-1390 |
| 7SSE | X-ray | 1.62 Å | A/B=1077-1390 |
| 9BHR | X-ray | 1.62 Å | A/B=1077-1390 |
| 9D4E | X-ray | 1.7 Å | A/B=1077-1390 |
| 4PXW | X-ray | 1.72 Å | A/B=1039-1401 |
| 9YE4 | X-ray | 1.74 Å | A/B=1080-1390 |
| 9C1Q | X-ray | 1.8 Å | A=1077-1390 |
| 9NSN | X-ray | 1.85 Å | B=1080-1390 |
| 9NSO | X-ray | 1.85 Å | B=1080-1390 |
| 7UFV | X-ray | 1.9 Å | A/B=1077-1390 |
| 9B9W | X-ray | 1.92 Å | B=1080-1390 |
| 9B9T | X-ray | 2.05 Å | B=1080-1390 |
| 9B9H | X-ray | 2.06 Å | B=1080-1390 |
Showing 20 of 43 experimental structures (best resolution first).
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