5ztn

X-ray diffraction
2.5Å resolution

The crystal structure of human DYRK2 in complex with Curcumin

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-187713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity tyrosine-phosphorylation-regulated kinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 429 amino acids
Theoretical weight: 49.52 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

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P42
Unit cell:
a: 83.659Å b: 83.659Å c: 149.127Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.244
Expression system: Escherichia coli BL21(DE3)