Research workbench
Crystal structure of maize CK2 alpha in complex with emodin at 1.92 a resolution
Analyse Crystal structure of maize CK2 alpha in complex with emodin at 1.92 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PZH
- Type
- protein
- Length
- 328 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
- EMO, CL
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase II subunit alpha (EC 2.7.11.1) | protein | 328 | 45% helix, 15% strand | P28523 |
Ligands and binding sites
- EMO · 3-methyl-1,6,8-trihydroxyanthraquinone · ligand · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
- ACT · Acetate ion · additive · 2 copies · 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 | 335 | 0.67 | 0.81 | 41 | EMO |
| 2 | 60 | 0.33 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 modified (artifact).
Compared structures
- 3PZH · Crystal structure of maize CK2 alpha in complex with emodin at 1.92 A resolution · 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 3PZH · PDBe 3PZH · UniProt P28523
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