Research workbench
Crystal structure of human CDK8-cyclin C in complex with cortistatin a
Analyse Crystal structure of human CDK8-cyclin C in complex with cortistatin a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CRL
- Type
- protein
- Length
- 605 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclin-dependent kinase 8; Cyclin-C
- EC
- 2.7.11.22
- UniProt
- P49336, P24863
- Ligands
- C1I
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclin-dependent kinase 8 (EC 2.7.11.22) | protein | 339 | 40% helix, 13% strand | P49336 |
| B | Cyclin-C | protein | 266 | 69% helix, 0% strand | P24863 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.71 | 0.81 | 50 | C1I, FMT |
| 2 | 252 | 0.61 | 0.80 | 35 | empty |
| 3 | 199 | 0.54 | 0.78 | 23 | empty |
| 4 | 72 | 0.52 | 0.86 | 17 | empty |
| 5 | 200 | 0.50 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1880 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4CRL · Crystal structure of human CDK8-Cyclin C in complex with cortistatin A · the same entry in another collection · chain A against A, TM-score 1.00
- P24863 · AlphaFold monomer V2.0 prediction for cyclin-C (P24863) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P49336 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 8 (P49336) · a predicted model of the same protein · chain A 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 P49336
- Every structure of UniProt P24863
- Elsewhere: RCSB PDB 4CRL · PDBe 4CRL · UniProt P49336 · UniProt P24863
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