MolNFT v1 · #172974 · protein
Structure of DYRK2 in complex with compound 50
7AKF · Dual specificity tyrosine-phosphorylation-regulated kinase 2: “Structure of DYRK2 in complex with compound 50”. X-ray diffraction, 2 ligands (RK5, CL), 4 pockets (best druggability 0.64). MolNFT v1 #172974 on GenesisL1: 3D…
- PDB
- 7AKF
- Type
- protein
- Length
- 402 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
- RK5, CL
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 34% 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 | 402 | 34% helix, 19% strand | Q92630 |
Ligands and binding sites
- RK5 · 4-(2,3-dimethyl-1-benzofuran-5-yl)pyridine-2,6-diamine · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 221 | 0.64 | 0.82 | 28 | RK5 |
| 2 | 192 | 0.54 | 0.79 | 29 | empty |
| 3 | 51 | 0.34 | 0.79 | 19 | empty |
| 4 | 62 | 0.31 | 0.75 | 13 | empty |
Modifications
Observed in the structure: 3 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 7AKF · PDBe 7AKF · UniProt Q92630
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