MolNFT v1 · #172958 · protein
Structure of DYRK1A in complex with compound 51
7AJY · Dual specificity tyrosine-phosphorylation-regulated kinase…: “Structure of DYRK1A in complex with compound 51”. X-ray diffraction, 2 ligands (RKZ, CL), 5 pockets (best druggability 0.83). MolNFT v1 #172958 on GenesisL1: 3D…
- PDB
- 7AJY
- Type
- protein
- Length
- 663 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- EC
- 2.7.12.1
- UniProt
- Q13627
- Ligands
- RKZ, CL
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 335 | 36% helix, 17% strand | Q13627 |
| B | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 328 | 36% helix, 18% strand | Q13627 |
Ligands and binding sites
- RKZ · 4-[2-methyl-3-[(2~{R})-2-phenoxypropyl]imidazo[4,5-b]pyridin-5-yl]pyridine-2,6-diamine · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 854 | 0.83 | 0.85 | 88 | RKZ |
| 2 | 194 | 0.66 | 0.84 | 25 | RKZ |
| 3 | 86 | 0.44 | 0.80 | 20 | empty |
| 4 | 71 | 0.42 | 0.80 | 17 | empty |
| 5 | 54 | 0.34 | 0.78 | 16 | CL |
Interfaces
1 interface between chains.
- A–B · 791 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 Q13627
- Elsewhere: RCSB PDB 7AJY · PDBe 7AJY · UniProt Q13627
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