Research workbench
Crystal structure of the alpha subunit of protein kinase CK2 in complex with the nucleotide competitive inhibitor emodin
Analyse Crystal structure of the alpha subunit of protein kinase CK2 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F0Q
- Type
- protein
- Length
- 329 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
- EMO
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein kinase CK2, alpha subunit (EC 2.7.1.37) | protein | 329 | 39% helix, 12% strand | P28523 |
Ligands and binding sites
- EMO · 3-methyl-1,6,8-trihydroxyanthraquinone · ligand · 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 | 162 | 0.69 | 0.88 | 30 | EMO |
| 2 | 79 | 0.40 | 0.79 | 19 | empty |
Compared structures
- 1F0Q · Crystal structure of the alpha subunit of protein kinase CK2 in complex with the… · 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 0.98
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 P28523
- Elsewhere: RCSB PDB 1F0Q · PDBe 1F0Q · UniProt P28523
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