Research workbench
Crystal structure of protein kinase CK2 in complex with tbb- derivatives inhibitors
Analyse Crystal structure of protein kinase CK2 in complex with tbb- derivatives… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZOE
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein kinase CK2, alpha subunit
- EC
- 2.7.1.37
- UniProt
- P28523
- Ligands
- K25, CL
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase CK2, alpha subunit (EC 2.7.1.37) | protein | 325 | 42% helix, 15% strand | P28523 |
Ligands and binding sites
- K25 · 4,5,6,7-tetrabromo-N,N-dimethyl-1H-benzimidazol-2-amine · ligand · chains A
- CL · Chloride ion · ion · chains A
- DMS · Dimethyl sulfoxide · 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 | 440 | 0.69 | 0.80 | 55 | CL, K25, DMS |
| 2 | 53 | 0.61 | 0.92 | 20 | empty |
| 3 | 62 | 0.33 | 0.76 | 17 | empty |
Compared structures
- 1ZOE · Crystal structure of protein kinase CK2 in complex with TBB-derivatives inhibitors · 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 1ZOE · PDBe 1ZOE · UniProt P28523
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