› 5lxd

X-ray diffraction
2.58Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187711 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity tyrosine-phosphorylation-regulated kinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 408 amino acids
Theoretical weight: 46.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92630 (Residues: 146-552; Coverage: 68%)
Gene name: DYRK2
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:
Ligand 7A7 2 x 7A7
Ligand EDO 10 x EDO
1 modified residue:
Ligand PTR 2 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: C2
Unit cell:
a: 66.24Å b: 130Å c: 136.33Å
α: 90° β: 90.4° γ: 90°
R-values:
R R work R free
0.2 0.197 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.
Nguyen et al. (2017)
4 more

4 mentions without citation

Dual-Specificity, Tyrosine Phosphorylation-Regulated Kinases (DYRKs) and cdc2-Like Kinases (CLKs) in Human Disease, an Overview.
Lindberg et al. (2021)
3 more