3k2l

X-ray diffraction
2.36Å resolution

Crystal Structure of dual-specificity tyrosine phosphorylation regulated kinase 2 (DYRK2)

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-187711 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity tyrosine-phosphorylation-regulated kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 429 amino acids
Theoretical weight: 49.76 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
Structure domains:

Ligands and Environments

3 bound ligands:
3 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P42212
Unit cell:
a: 84.285Å b: 84.285Å c: 148.505Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.225 0.288
Expression system: Escherichia coli BL21(DE3)