MolNFT v1 · #105984 · protein
Crystal structure of Z. mays CK2ALPHA in complex with the ATP- competitive inhibitor 4-[(E)-(fluoren-9-ylidenehydrazinylidene)- methyl] benzoate
4RLK · Casein kinase II subunit alpha: “Crystal structure of Z. mays CK2ALPHA in complex with the ATP- competitive inhibitor…”. X-ray diffraction, 1 ligand (E91), 2 pockets (best druggability 0.72). MolNFT v1 #105984 on GenesisL1: 3D…
- PDB
- 4RLK
- Type
- protein
- Length
- 327 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
- E91
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Casein kinase II subunit alpha (EC 2.7.11.1) | protein | 327 | 46% helix, 16% strand | P28523 |
Ligands and binding sites
- E91 · 4-[(E)-(9H-fluoren-9-ylidenehydrazinylidene)methyl]benzoic acid · ligand · chains A
- GOL · Glycerol · additive · 3 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 | 392 | 0.72 | 0.83 | 48 | GOL, E91 |
| 2 | 57 | 0.31 | 0.76 | 12 | empty |
Compared structures
- 4RLK · Crystal structure of Z. mays CK2alpha in complex with the ATP-competitive inhibitor… · 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 4RLK · PDBe 4RLK · UniProt P28523
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