Cyclin-dependent kinase 7 (CDK7) is a 346-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P50613.
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The mean pLDDT of this model is 82.0 (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 | 9% |
| Below 50 | Very low: often disordered regions | 16% |
What pLDDT means and how to read it
Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription (PubMed:9852112, PubMed:19136461, PubMed:26257281, PubMed:28768201). As a cyclin-dependent kinase, CDK7 is activated by the binding to cyclin-H/CCNH and the CDK-activating kinase assembly factor MAT1 (PubMed:41100585). Catalytic subunit of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs (PubMed:41100585). CAK activates major mediators of cell cycle control, including CDK1, CDK2, CDK4 and CDK6, and plays a key role in regulating cell cycle progression (PubMed:41100585). CAK complexed to the…
Component of the CDK-activating kinase (CAK) complex, consisting of CDK7, cyclin-H/CCNH and MAT1, which is a master regulator of CDK activity (PubMed:41100585). CAK binds to both free CDK2 and cyclin-bound CDK2, with a higher affinity for the cyclin-bound form (PubMed:41100585). CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor (PubMed:9852112). The CAK…
Nucleus, Cytoplasm, Cytoplasm, perinuclear region
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8P79 | EM | 1.7 Å | J=1-346 |
| 8R9A | X-ray | 1.71 Å | A=1-346 |
| 8P77 | EM | 1.8 Å | J=1-346 |
| 8R99 | X-ray | 1.81 Å | A=1-346 |
| 8ORM | EM | 1.9 Å | J=1-346 |
| 8P6V | EM | 1.9 Å | J=1-346 |
| 8P6W | EM | 1.9 Å | J=1-346 |
| 8P6X | EM | 1.9 Å | J=1-346 |
| 8P6Y | EM | 1.9 Å | J=1-346 |
| 8P72 | EM | 1.9 Å | J=1-346 |
| 8P78 | EM | 1.9 Å | J=1-346 |
| 8PLZ | EM | 1.9 Å | J=1-346 |
| 8R9U | X-ray | 1.94 Å | A/B=1-346 |
| 8P70 | EM | 2.0 Å | J=1-346 |
| 8P71 | EM | 2.0 Å | J=1-346 |
| 8P73 | EM | 2.0 Å | J=1-346 |
| 8P75 | EM | 2.0 Å | J=1-346 |
| 8P76 | EM | 2.0 Å | J=1-346 |
| 8P6Z | EM | 2.1 Å | J=1-346 |
| 8P7L | EM | 2.1 Å | J=1-346 |
Showing 20 of 54 experimental structures (best resolution first).
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