› 6fyi

X-ray diffraction
2.6Å 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-156011 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK2 Chain: A
Molecule details ›
Chain: A
Length: 368 amino acids
Theoretical weight: 43.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P49760 (Residues: 132-496; Coverage: 73%)
Gene name: CLK2
Sequence domains: Protein kinase domain
Structure domains: Phosphorylase Kinase; domain 1

Ligands and Environments

1 bound ligand:
Ligand EAE 1 x EAE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 39.444Å b: 76.531Å c: 111.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.218 0.233
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

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

1 mention without citation

Structural Basis of Inhibitor Selectivity in the BRD7/9 Subfamily of Bromodomains.
Karim et al. (2020)