Cyclin-T1 (CCNT1) is a 726-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O60563.
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The mean pLDDT of this model is 59.4 (low 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 | 29% |
| 70 to 90 | Confident: backbone generally right | 9% |
| 50 to 70 | Low: treat with caution | 9% |
| Below 50 | Very low: often disordered regions | 53% |
What pLDDT means and how to read it
Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) 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 (RNA Pol II) (PubMed:16109376, PubMed:16109377, PubMed:30134174, PubMed:35393539). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II (PubMed:29849146, PubMed:35393539)
Cyclin-T1 is the predominant cyclin that associates with CDK9 to form a heterodimer called P-TEFb (PubMed:30134174, PubMed:35393539, PubMed:9499409). P-TEFb forms a complex with AFF4/AF5Q31 (PubMed:12065898). Component of a complex which is at least composed of HTATSF1/Tat-SF1, P-TEFb complex, RNA pol II, SUPT5H, and NCL/nucleolin (PubMed:10393184). Component of the 7SK snRNP complex at least…
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 3MI9 | X-ray | 2.1 Å | B=1-266 |
| 3BLH | X-ray | 2.48 Å | B=2-259 |
| 2PK2 | X-ray | 2.67 Å | A/B/C/D=1-281 |
| 3BLR | X-ray | 2.8 Å | B=2-259 |
| 3MY1 | X-ray | 2.8 Å | B=2-259 |
| 7NWK | X-ray | 2.81 Å | B=2-259 |
| 3BLQ | X-ray | 2.9 Å | B=2-259 |
| 4OR5 | X-ray | 2.9 Å | B/G=1-266 |
| 4IMY | X-ray | 2.94 Å | B/D/F=1-264 |
| 3TN8 | X-ray | 2.95 Å | B=2-259 |
| 4BCH | X-ray | 2.96 Å | B=2-259 |
| 3LQ5 | X-ray | 3.0 Å | B=2-259 |
| 3MIA | X-ray | 3.0 Å | B=1-266 |
| 4OGR | X-ray | 3.0 Å | B/F/K=1-264 |
| 4BCF | X-ray | 3.01 Å | B=2-259 |
| 4BCG | X-ray | 3.08 Å | B=2-259 |
| 4BCI | X-ray | 3.1 Å | B=2-259 |
| 6W9E | X-ray | 3.1 Å | B=1-259 |
| 4BCJ | X-ray | 3.16 Å | B=2-259 |
| 6GZH | X-ray | 3.17 Å | B=1-726 |
Showing 20 of 29 experimental structures (best resolution first).
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