Research workbench
Complex structure of human protein kinase CK2 catalytic subunit crystallized in the presence of a bisubstrate inhibitor
Analyse Complex structure of human protein kinase CK2 catalytic subunit crystallized in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FBX
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.33
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Casein kinase II subunit alpha; bisubstrate inhibitor
- EC
- 2.7.11.1
- UniProt
- P68400
- Ligands
- CL
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · resolution 2.33 · 2 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase II subunit alpha (EC 2.7.11.1) | protein | 333 | 40% helix, 15% strand | P68400 |
| B | bisubstrate inhibitor | protein | 1 | 0% helix, 0% strand | — |
Ligands and binding sites
- CL · Chloride ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.52 | 0.78 | 30 | CL |
Interfaces
1 interface between chains.
- A–B · 333 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 4FBX · Complex structure of human protein kinase CK2 catalytic subunit crystallized in the… · the same entry in another collection · chain A against A, TM-score 1.00
- P68400 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha (P68400) · 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 P68400
- Elsewhere: RCSB PDB 4FBX · PDBe 4FBX · UniProt P68400
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