Cyclin-A2 (CCNA2) is a 432-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P20248.
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The mean pLDDT of this model is 73.1 (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 | 58% |
| 70 to 90 | Confident: backbone generally right | 2% |
| 50 to 70 | Low: treat with caution | 3% |
| Below 50 | Very low: often disordered regions | 37% |
What pLDDT means and how to read it
Essential for the control of the cell cycle at G1/S and G2/M transition (PubMed:1312467). Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle (PubMed:41100585)
Interacts with the CDK1 and CDK2 protein kinases to form serine/threonine kinase holoenzyme complexes (PubMed:1312467, PubMed:7630397, PubMed:8684460, PubMed:8756328, PubMed:41100585). Interacts with CDK1 (hyperphosphorylated form in G1 and underphosphorylated forms in S and G2) (PubMed:1312467). Interacts with CDK2; the interaction increases from G1 to G2 (PubMed:1312467). Interacts (associated…
Nucleus, Cytoplasm
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9D97 | X-ray | 1.6 Å | C=178-186 |
| 4EOJ | X-ray | 1.65 Å | B/D=175-432 |
| 2CCH | X-ray | 1.7 Å | B/D=173-432 |
| 7QHL | X-ray | 1.7 Å | B/D=175-432 |
| 7ACK | X-ray | 1.8 Å | B/D=175-432 |
| 6ATH | X-ray | 1.82 Å | B=173-432 |
| 4EOP | X-ray | 1.99 Å | B/D=175-432 |
| 1H1R | X-ray | 2.0 Å | B/D=175-432 |
| 1H1S | X-ray | 2.0 Å | B/D=175-432 |
| 1OIU | X-ray | 2.0 Å | B/D=174-432 |
| 2IW9 | X-ray | 2.0 Å | B/D=174-432 |
| 4CFV | X-ray | 2.0 Å | B/D=172-432 |
| 4EOI | X-ray | 2.0 Å | B/D=175-432 |
| 5CYI | X-ray | 2.0 Å | B/D=174-432 |
| 4BCK | X-ray | 2.05 Å | B/D=171-432 |
| 2UUE | X-ray | 2.06 Å | B/D=174-432 |
| 1H1P | X-ray | 2.1 Å | B/D=175-432 |
| 1OI9 | X-ray | 2.1 Å | B/D=174-432 |
| 2C5N | X-ray | 2.1 Å | B/D=174-432 |
| 2C5O | X-ray | 2.1 Å | B/D=173-432 |
Showing 20 of 114 experimental structures (best resolution first).
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