Cell division cycle protein 20 homolog (CDC20) is a 499-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12834.
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The mean pLDDT of this model is 84.1 (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 | 62% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 15% |
| Below 50 | Very low: often disordered regions | 10% |
What pLDDT means and how to read it
Substrate-specific adapter and activator of the anaphase promoting complex/cyclosome (APC/C) that confers substrate specificity by binding to substrates and targeting them to the APC/C for ubiquitination and degradation (PubMed:9734353, PubMed:27030811, PubMed:29343641, PubMed:27120157, PubMed:27509861). Essential for activating APC/C in the metaphase/anaphase transition of the cell cycle, targeting the degradation of cyclin B and securin (PubMed:27120157, PubMed:27509861, PubMed:32666501). Recognizes and binds the destruction box (D box), KEB box and ABBA motifs on protein substrates (PubMed:29343641, PubMed:27509861). The CDC20-APC/C complex positively regulates the formation of synaptic…
Associates with phosphorylated anaphase promoting complex/cyclosome (APC/C) to form the CDC20-APC/C complex, which is crucial for metaphase/anaphase transition in cell cycle; this interaction is dependent on APC/C phosphorylation (PubMed:27120157, PubMed:27509861). Within the CDC20-APC/C complex, interacts (via KILR motif and C-box motif) with CDC23/ANAPC8 and (via IR tail) CDC27/ANAPC3…
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Chromosome, centromere, kinetochore, Cytoplasm, cytoskeleton, spindle pole
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4GGC | X-ray | 1.35 Å | A=161-477 |
| 9I69 | X-ray | 1.46 Å | A=1-499 |
| 9I68 | X-ray | 1.5 Å | A=1-499 |
| 9I6A | X-ray | 1.92 Å | A=1-499 |
| 4GGA | X-ray | 2.04 Å | A=81-499 |
| 4N14 | X-ray | 2.1 Å | A=165-477 |
| 4GGD | X-ray | 2.44 Å | A/B=71-499 |
| 6Q6G | EM | 3.2 Å | R=1-499 |
| 6Q6H | EM | 3.2 Å | R=1-499 |
| 6TLJ | EM | 3.8 Å | Q=126-499, R=1-499 |
| 9N9R | EM | 3.9 Å | R=1-499 |
| 9N9S | EM | 3.9 Å | R=1-499 |
| 5G04 | EM | 4.0 Å | R=1-499 |
| 5LCW | EM | 4.0 Å | Q=126-499, R=1-499 |
| 6F0X | EM | 4.6 Å | Q=1-499 |
| 5KHU | EM | 4.8 Å | R/S=1-499 |
| 5KHR | EM | 6.1 Å | R=1-499 |
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