Cyclin-dependent kinase 2 (CDK2) is a 298-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P24941.
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The mean pLDDT of this model is 88.4 (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 | 69% |
| 70 to 90 | Confident: backbone generally right | 20% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 3% |
What pLDDT means and how to read it
Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis (PubMed:10499802, PubMed:10884347, PubMed:10995386, PubMed:10995387, PubMed:11051553, PubMed:11113184, PubMed:12944431, PubMed:15800615, PubMed:17495531, PubMed:19966300, PubMed:20935635, PubMed:21262353, PubMed:21596315, PubMed:28216226, PubMed:28666995). Phosphorylates CABLES1, CTNNB1, CDK2AP2, ERCC6, NBN, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, SUV39H1, EZH2 (PubMed:10499802, PubMed:10995386, PubMed:10995387, PubMed:11051553, PubMed:11113184, PubMed:12944431, PubMed:15800615, PubMed:19966300, PubMed:20935635, PubMed:21262353, PubMed:21596315,…
Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 (By similarity). Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC (PubMed:15611625). Interaction with SPDYA promotes kinase activation via a conformation change that alleviates obstruction of the substrate-binding cleft by the T-loop…
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Nucleus, Cajal body, Cytoplasm, Endosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6Q4G | X-ray | 0.98 Å | A=1-298 |
| 6Q49 | X-ray | 1.0 Å | A=1-298 |
| 6Q4H | X-ray | 1.0 Å | A=1-298 |
| 6Q48 | X-ray | 1.03 Å | A=1-298 |
| 6Q4J | X-ray | 1.05 Å | A=1-298 |
| 6Q4E | X-ray | 1.06 Å | A=1-298 |
| 6Q4K | X-ray | 1.06 Å | A=1-298 |
| 6Q4D | X-ray | 1.07 Å | A=1-298 |
| 6Q3B | X-ray | 1.11 Å | A=1-298 |
| 6Q4I | X-ray | 1.11 Å | A=1-298 |
| 6Q4B | X-ray | 1.12 Å | A=1-298 |
| 6Q4A | X-ray | 1.13 Å | A=1-298 |
| 9GNO | X-ray | 1.16 Å | A=1-298 |
| 6Q3F | X-ray | 1.18 Å | A=1-298 |
| 6Q4F | X-ray | 1.21 Å | A=1-298 |
| 4EK4 | X-ray | 1.26 Å | A=1-298 |
| 4FKL | X-ray | 1.26 Å | A=1-298 |
| 2R3I | X-ray | 1.28 Å | A=1-298 |
| 6Q3C | X-ray | 1.29 Å | A=1-298 |
| 1GZ8 | X-ray | 1.3 Å | A=1-298 |
Showing 20 of 521 experimental structures (best resolution first).
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