Cell division control protein 48 (CDC48) is a 835-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P25694.
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The mean pLDDT of this model is 79.1 (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 | 29% |
| 70 to 90 | Confident: backbone generally right | 52% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:21454554, PubMed:31445887). By recruiting and promoting the degradation of ubiquitinated proteins, plays a role in the ubiquitin fusion degradation (UFD) pathway (PubMed:16428438). Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway which mediates the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:11740563, PubMed:11813000, PubMed:11847109, PubMed:21148305). Required for the proteasome-dependent processing/activation of MGA2…
Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the complexes is mediated by interaction between…
Endoplasmic reticulum, Cytoplasm, cytosol, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8UB4 | EM | 2.9 Å | A/B/C/D/E/F=1-835 |
| 8DAR | EM | 3.0 Å | A/B/C/D/E/F=1-835 |
| 9OFV | EM | 3.16 Å | A/B/C/D/E/F=1-835 |
| 8U9P | EM | 3.2 Å | A/B/C/D/E/F=1-835 |
| 8U7T | EM | 3.3 Å | A/B/C/D/E/F=1-835 |
| 8UA1 | EM | 3.4 Å | A/B/C/D/E/F=1-835 |
| 8UAA | EM | 3.4 Å | A/B/C/D/E/F=1-835 |
| 8DAS | EM | 3.5 Å | A/B/C/D/E/F=1-835 |
| 8DAV | EM | 3.5 Å | A/B/C/D/E/F=1-835 |
| 8U8I | EM | 3.5 Å | A/B/C/D/E/F=1-835 |
| 8UA0 | EM | 3.5 Å | A/B/C/D/E/F=1-835 |
| 6OAB | EM | 3.6 Å | A/B/C/D/E=1-835 |
| 8DAW | EM | 3.6 Å | A/B/C/D/E/F=1-835 |
| 6OMB | EM | 3.7 Å | A/B/C/D/E=1-835 |
| 6OPC | EM | 3.7 Å | A/B/C/D/E/F=1-835 |
| 8DAU | EM | 3.7 Å | A/B/C/D/E/F=1-835 |
| 8U9C | EM | 3.7 Å | A/B/C/D/E/F=1-835 |
| 8DAT | EM | 3.8 Å | A/B/C/D/E/F=1-835 |
| 8U9Z | EM | 3.8 Å | A/B/C/D/E/F=1-835 |
| 6OA9 | EM | 3.9 Å | A/B/C/D/E/F=1-835 |
Showing 20 of 22 experimental structures (best resolution first).
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