Cyclin-dependent kinase 9 (CDK9) is a 372-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50750.
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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 | 72% |
| 70 to 90 | Confident: backbone generally right | 13% |
| 50 to 70 | Low: treat with caution | 7% |
| Below 50 | Very low: often disordered regions | 9% |
What pLDDT means and how to read it
Protein kinase involved in the regulation of transcription (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399, PubMed:14701750, PubMed:16109376, PubMed:16109377, PubMed:20930849, PubMed:28426094, PubMed:29335245). Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP (PubMed:10574912, PubMed:10757782, PubMed:11145967, PubMed:11575923, PubMed:11809800, PubMed:11884399,…
Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Associates with CCNT1/cyclin-T1, CCNT2/cyclin-T2 (isoform A and isoform B) or CCNK/cyclin-K to form active P-TEFb. P-TEFb forms a complex with AFF4/AF5Q31 and is part of the super elongation complex (SEC). Component of a complex…
Nucleus, Cytoplasm, Nucleus, PML body
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3MI9 | X-ray | 2.1 Å | A=1-345 |
| 3BLH | X-ray | 2.48 Å | A=2-330 |
| 3BLR | X-ray | 2.8 Å | A=2-330 |
| 3MY1 | X-ray | 2.8 Å | A=2-330 |
| 7NWK | X-ray | 2.81 Å | A=1-330 |
| 3BLQ | X-ray | 2.9 Å | A=2-330 |
| 4OR5 | X-ray | 2.9 Å | A/F=7-332 |
| 4IMY | X-ray | 2.94 Å | A/C/E=1-330 |
| 3TN8 | X-ray | 2.95 Å | A=2-330 |
| 4BCH | X-ray | 2.96 Å | A=2-330 |
| 3LQ5 | X-ray | 3.0 Å | A=2-330 |
| 3MIA | X-ray | 3.0 Å | A=1-345 |
| 4OGR | X-ray | 3.0 Å | A/E/I=1-330 |
| 4BCF | X-ray | 3.01 Å | A=2-330 |
| 4BCG | X-ray | 3.08 Å | A=2-330 |
| 4BCI | X-ray | 3.1 Å | A=2-330 |
| 6W9E | X-ray | 3.1 Å | A=1-330 |
| 4BCJ | X-ray | 3.16 Å | A=2-330 |
| 6GZH | X-ray | 3.17 Å | A=1-326 |
| 3TNH | X-ray | 3.2 Å | A=2-330 |
Showing 20 of 28 experimental structures (best resolution first).
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