CDK-activating kinase assembly factor MAT1 (MNAT1) is a 309-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P51948.
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The mean pLDDT of this model is 85.4 (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 | 43% |
| 70 to 90 | Confident: backbone generally right | 45% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 2% |
What pLDDT means and how to read it
Component of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs (PubMed:41100585). Binds and activates CDK7, the catalytic subunit of CAK (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 core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts (PubMed:10024882). Involved…
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 can further associate with the core-TFIIH to form the TFIIH basal transcription factor (PubMed:9852112)
Nucleus
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 8P79 | EM | 1.7 Å | H=220-309 |
| 8P77 | EM | 1.8 Å | H=220-309 |
| 8ORM | EM | 1.9 Å | H=220-309 |
| 8P6V | EM | 1.9 Å | H=220-309 |
| 8P6W | EM | 1.9 Å | H=220-309 |
| 8P6X | EM | 1.9 Å | H=220-309 |
| 8P6Y | EM | 1.9 Å | H=220-309 |
| 8P72 | EM | 1.9 Å | H=220-309 |
| 8P78 | EM | 1.9 Å | H=220-309 |
| 8PLZ | EM | 1.9 Å | H=220-309 |
| 8P70 | EM | 2.0 Å | H=220-309 |
| 8P71 | EM | 2.0 Å | H=220-309 |
| 8P73 | EM | 2.0 Å | H=220-309 |
| 8P75 | EM | 2.0 Å | H=220-309 |
| 8P76 | EM | 2.0 Å | H=220-309 |
| 6TUN | X-ray | 2.07 Å | C/D=66-141 |
| 8P6Z | EM | 2.1 Å | H=220-309 |
| 8P7L | EM | 2.1 Å | H=1-309 |
| 8PYR | X-ray | 2.15 Å | C/G=230-309 |
| 8P74 | EM | 2.2 Å | H=220-309 |
Showing 20 of 67 experimental structures (best resolution first).
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