Research workbench
Human CK2 catalytic domain in complex with a pyridocarbazole derivative inhibitor
Analyse Human CK2 catalytic domain in complex with a pyridocarbazole derivative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OWJ
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSNK2A1 protein
- UniProt
- Q5U5J2
- Ligands
- 1EL
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSNK2A1 protein | protein | 328 | 39% helix, 15% strand | Q5U5J2 |
Ligands and binding sites
- 1EL · 9-hydroxy-5,11-dimethyl-4,6-dihydro-1H-pyrido[4,3-b]carbazol-1-one · 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 | 317 | 0.68 | 0.82 | 38 | 1EL |
| 2 | 63 | 0.30 | 0.74 | 16 | empty |
Compared structures
- 3OWJ · Human CK2 catalytic domain in complex with a pyridocarbazole derivative inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5U5J2
- Elsewhere: RCSB PDB 3OWJ · PDBe 3OWJ · UniProt Q5U5J2
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