› 6fyv

X-ray diffraction
2.46Å 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-190730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK4 Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 39.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9HAZ1 (Residues: 146-480; Coverage: 70%)
Gene name: CLK4
Sequence domains: Protein kinase domain
Structure domains: Phosphorylase Kinase; domain 1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P43212
Unit cell:
a: 66.335Å b: 66.335Å c: 190.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.203 0.223
Expression system: Escherichia coli BL21

Quick links

Citations

3 citation in other articles

Structural Basis for the Selective Inhibition of Cdc2-Like Kinases by CX-4945.
Lee et al. (2019)
2 more

7 mentions without citation

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