Research workbench
Crystal structure of full-length CDK9 in complex with cyclin T
Analyse Crystal structure of full-length CDK9 in complex with cyclin T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EC9
- Type
- protein
- Length
- 558 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent kinase 9; Cyclin-T1
- EC
- 2.7.11.22, 2.7.11.23
- UniProt
- P50750, O60563
- Pockets
- 10 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent kinase 9 (EC 2.7.11.22, 2.7.11.23) | protein | 307 | 35% helix, 15% strand | P50750 |
| B | Cyclin-T1 | protein | 251 | 64% helix, 0% strand | O60563 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.62 | 0.79 | 35 | empty |
| 2 | 185 | 0.55 | 0.79 | 22 | empty |
| 3 | 161 | 0.48 | 0.77 | 23 | empty |
| 4 | 105 | 0.46 | 0.79 | 13 | empty |
| 5 | 113 | 0.45 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 877 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 4EC9 · Crystal structure of full-length cdk9 in complex with cyclin t · the same entry in another collection · chain A against A, TM-score 1.00
- P50750 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 9 (P50750) · a predicted model of the same protein · chain A against A, TM-score 0.98
- O60563 · AlphaFold monomer V2.0 prediction for cyclin-T1 (O60563) · a predicted model of the same protein · chain B against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P50750
- Every structure of UniProt O60563
- Elsewhere: RCSB PDB 4EC9 · PDBe 4EC9 · UniProt P50750 · UniProt O60563
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