Research workbench
Crystal structure of Z. mays CK2 kinase alpha subunit in complex with the inhibitor (2-dymethylammino-4,5,6,7-tetrabromobenzoimidazol-1YL- acetic acid (K66)
Analyse Crystal structure of Z. mays CK2 kinase alpha subunit in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KXH
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Casein kinase II subunit alpha
- EC
- 2.7.11.1
- UniProt
- P28523
- Ligands
- K66
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase II subunit alpha (EC 2.7.11.1) | protein | 327 | 42% helix, 15% strand | P28523 |
Ligands and binding sites
- K66 · [4,5,6,7-tetrabromo-2-(dimethylamino)-1H-benzimidazol-1-yl]acetic acid · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.70 | 0.81 | 44 | K66 |
| 2 | 50 | 0.63 | 0.94 | 18 | empty |
| 3 | 71 | 0.39 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 3KXH · Crystal structure of Z. mays CK2 kinase alpha subunit in complex with the inhibitor… · the same entry in another collection · chain A against A, TM-score 1.00
- P28523 · AlphaFold monomer V2.0 prediction for casein kinase II subunit alpha (P28523) · 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 P28523
- Elsewhere: RCSB PDB 3KXH · PDBe 3KXH · UniProt P28523
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