X-ray diffraction
2.35Å resolution

Crystal structure of the phosphorylated CLK3

Source organism: Homo sapiens
Entry authors: Papagrigoriou E, Rellos P, Das S, Bullock A, Ball LJ, Turnbull A, Savitsky P, Fedorov O, Johansson C, Ugochukwu E, Sobott F, von Delft F, Edwards A, Sundstrom M, Weigelt J, Arrowsmith C, Knapp S, Structural Genomics Consortium (SGC)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Dual specificity protein kinase CLK3 Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P49761 (Residues: 275-631; Coverage: 56%)
Gene name: CLK3
Sequence domains: Protein kinase domain
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: I222
Unit cell:
a: 62.18Å b: 110.998Å c: 161.544Å
α: 90° β: 90° γ: 90°
R R work R free
0.227 0.225 0.26
Expression system: Escherichia coli BL21(DE3)