CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.510 | Transferase(Phosphotransferase); domain 1 |
|
1.10.510.10 | Transferase(Phosphotransferase) domain 1 |
Domain Context
CATH Clusters
| Superfamily | Transferase(Phosphotransferase) domain 1 |
| Functional Family | Cyclin-dependent kinase 9 |
Enzyme Information
| 2.7.11.23 |
[RNA-polymerase]-subunit kinase.
based on mapping to UniProt P50750
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
-!- Appears to be distinct from other protein phosphokinases. -!- Brings about multiple phosphorylation of the unique C-terminal repeat domain of the largest subunit of eukaryotic EC 2.7.7.6. -!- Does not phosphorylate casein, phosvitin or histone. -!- Formerly EC 2.7.1.141.
|
| 2.7.11.22 |
Cyclin-dependent kinase.
based on mapping to UniProt P50750
ATP + a protein = ADP + a phosphoprotein.
-!- Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. -!- It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation. -!- Formerly EC 2.7.1.37.
|
UniProtKB Entries (1)
| P50750 |
CDK9_HUMAN
Homo sapiens
Cyclin-dependent kinase 9
|
PDB Structure
| PDB | 3TNI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The CDK9 C-helix Exhibits Conformational Plasticity That May Explain the Selectivity of CAN508.
Acs Chem.Biol.
|