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Crystal structure of human protein kinase CK2alpha' (CSNK2A2 gene product) in complex with the 2-aminothiazole-type inhibitor 27
Analyse Crystal structure of human protein kinase CK2alpha' (CSNK2A2 gene product) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TEW
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.082
- Source
- Homo sapiens
- Molecule
- Casein kinase II subunit alpha'
- EC
- 2.7.11.1
- UniProt
- P19784
- Ligands
- N5Q
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · resolution 1.082 · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase II subunit alpha' (EC 2.7.11.1) | protein | 325 | 41% helix, 16% strand | P19784 |
Ligands and binding sites
- N5Q · 4-[(4-naphthalen-2-yl-1,3-thiazol-2-yl)amino]-2-oxidanyl-benzoic acid · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · 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 | 350 | 0.68 | 0.81 | 46 | N5Q |
| 2 | 60 | 0.35 | 0.78 | 15 | empty |
Compared structures
- 6TEW · Crystal structure of human protein kinase CK2ALPHA' (CSNK2A2 gene product) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P19784 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha' (P19784) · 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 P19784
- Elsewhere: RCSB PDB 6TEW · PDBe 6TEW · UniProt P19784
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