7dho

X-ray diffraction
3.29Å resolution

The co-crystal structure of DYRK2 with a small molecule inhibitor 14

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: 324 amino acids
Theoretical weight: 37.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q92630 (Residues: 215-538; Coverage: 54%)
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: C2221
Unit cell:
a: 64.61Å b: 128.87Å c: 133.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.184 0.259
Expression system: Escherichia coli K-12