› 6fyl

X-ray diffraction
1.95Å 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: 363 amino acids
Theoretical weight: 42.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P49760 (Residues: 136-496; Coverage: 72%)
Gene name: CLK2
Sequence domains: Protein kinase domain
Structure domains: Phosphorylase Kinase; domain 1

Ligands and Environments

1 bound ligand:
Ligand 3NG 1 x 3NG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 39.631Å b: 75.997Å c: 111.701Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.213
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Cdc-Like Kinases (CLKs): Biology, Chemical Probes, and Therapeutic Potential.
Martín Moyano et al. (2020)
1 more

5 mentions without citation

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