Cullin-associated NEDD8-dissociated protein 1 (CAND1) is a 1230-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q86VP6.
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The mean pLDDT of this model is 86.8 (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 | 53% |
| 70 to 90 | Confident: backbone generally right | 40% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes
Interacts with TBP (By similarity). Part of a complex that contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated CUL1. Interaction with cullins is abolished in presence of COMMD1, which antagonizes with CAND1 for interacting with cullins. Interacts with ERCC6 (PubMed:26030138). Interacts with DCUN1D1,…
Cytoplasm, Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 7Z8R | EM | 2.7 Å | D=1-1230 |
| 7Z8V | EM | 2.7 Å | D=1-1230 |
| 8OR3 | EM | 2.9 Å | C=1-1230 |
| 7Z8T | EM | 3.0 Å | D=1-1230 |
| 1U6G | X-ray | 3.1 Å | C=1-1230 |
| 7ZBZ | EM | 3.1 Å | D=1-1230 |
| 8OR0 | EM | 3.1 Å | C=1-1230 |
| 8OR2 | EM | 3.2 Å | C=1-1230 |
| 8CDK | EM | 3.32 Å | D=1-1230 |
| 8CDJ | EM | 3.4 Å | D=1-1230 |
| 7ZBW | EM | 3.5 Å | D=1-1230 |
| 8H3Q | EM | 3.76 Å | A=1-1230 |
| 4A0C | X-ray | 3.8 Å | A/B=1-1230 |
| 8OR4 | EM | 3.8 Å | C=1-1230 |
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