› 6fyo

X-ray diffraction
2.32Å 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-156010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK1 Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 39.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P49759 (Residues: 148-484; Coverage: 70%)
Gene names: CLK, CLK1
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:
Ligand EAQ 1 x EAQ
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 62.039Å b: 49.511Å c: 65.514Å
α: 90° β: 117.55° γ: 90°
R-values:
R R work R free
0.204 0.203 0.234
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

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

1 mention without citation

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