Research workbench
Binary complex of casein kinase-1 from S. pombe with an ATP competitive inhibitor, IC261
Analyse Binary complex of casein kinase-1 from S. pombe with an ATP competitive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EH4
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Casein kinase-1
- EC
- 2.7.1.-
- UniProt
- P40233
- Ligands
- IC1, SO4
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Casein kinase-1 (EC 2.7.1.-) | protein | 293 | 35% helix, 15% strand | P40233 |
Ligands and binding sites
- IC1 · 3-[(2,4,6-trimethoxy-phenyl)-methylene]-indolin-2-one · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.63 | 0.82 | 28 | IC1 |
| 2 | 248 | 0.63 | 0.81 | 30 | IC1 |
| 3 | 186 | 0.60 | 0.82 | 37 | SO4 |
Interfaces
1 interface between chains.
- A–B · 424 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1EH4 · Binary complex of casein kinase-1 from S. pombe with an ATP competitive inhibitor, IC261 · the same entry in another collection · chain A against A, TM-score 1.00
- P40233 · AlphaFold monomer V2.0 prediction for casein kinase I homolog 1 (P40233) · 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 P40233
- Elsewhere: RCSB PDB 1EH4 · PDBe 1EH4 · UniProt P40233
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