6khe

X-ray diffraction
2.8Å resolution

Crystal structure of CLK2 in complex with CX-4945

Released:
Source organism: Homo sapiens
Primary publication:
Structural Basis for the Selective Inhibition of Cdc2-Like Kinases by CX-4945.
Biomed Res Int 2019 6125068 (2019)
PMID: 31531359

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 499 amino acids
Theoretical weight: 60.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49760 (Residues: 1-499; Coverage: 100%)
Gene name: CLK2
Sequence domains: Protein kinase domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P43212
Unit cell:
a: 75.627Å b: 75.627Å c: 161.825Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.196 0.261
Expression system: Escherichia coli