Research workbench
The co-crystal structure of DYRK2 with a small molecule inhibitor 10
Analyse The co-crystal structure of DYRK2 with a small molecule inhibitor 10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DHC
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity tyrosine-phosphorylation-regulated kinase 2
- EC
- 2.7.12.1
- UniProt
- Q92630
- Ligands
- H99
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) | protein | 324 | 35% helix, 20% strand | Q92630 |
Ligands and binding sites
- H99 · 4-[bis(fluoranyl)methyl]-2,7-dimethoxy-9-(piperidin-4-ylmethylsulfanyl)acridine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.65 | 0.78 | 51 | H99 |
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
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 Q92630
- Elsewhere: RCSB PDB 7DHC · PDBe 7DHC · UniProt Q92630
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