MolNFT v1 · #176271 · protein
The co-crystal structure of DYRK2 with a small molecule inhibitor 5
7DH3 · Dual specificity tyrosine-phosphorylation-regulated kinase 2: “The co-crystal structure of DYRK2 with a small molecule inhibitor 5”. X-ray diffraction, 1 ligand (H7C), 2 pockets (best druggability 0.67). MolNFT v1 #176271 on…
- PDB
- 7DH3
- Type
- protein
- Length
- 326 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
- H7C
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) | protein | 326 | 33% helix, 19% strand | Q92630 |
Ligands and binding sites
- H7C · 2,7-dimethoxy-9-piperidin-4-ylsulfanyl-acridine · 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 | 461 | 0.67 | 0.78 | 52 | H7C |
| 2 | 74 | 0.33 | 0.75 | 18 | empty |
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 7DH3 · PDBe 7DH3 · UniProt Q92630
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