Research workbench
Arabidopsis thaliana Casein Kinase 2 (CK2) alpha-1 crystal form I
Analyse Arabidopsis thaliana Casein Kinase 2 (CK2) alpha-1 crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XX6
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8492
- Source
- Arabidopsis thaliana
- Molecule
- Casein kinase II subunit alpha-1
- EC
- 2.7.11.1
- UniProt
- Q08467
- Ligands
- PIV, CL, SO4
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · resolution 1.8492 · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase II subunit alpha-1 (EC 2.7.11.1) | protein | 329 | 44% helix, 15% strand | Q08467 |
Ligands and binding sites
- PIV · Pivalic acid · ligand · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.65 | 0.84 | 41 | PIV |
| 2 | 60 | 0.44 | 0.83 | 17 | CL |
Compared structures
- 6XX6 · Arabidopsis thaliana casein kinase 2 (CK2) alpha-1 crystal form I · the same entry in another collection · chain A against A, TM-score 1.00
- Q08467 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha-1 (Q08467) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q08467
- Elsewhere: RCSB PDB 6XX6 · PDBe 6XX6 · UniProt Q08467
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