3nr9

X-ray diffraction
2.89Å resolution

Structure of human CDC2-like kinase 2 (CLK2)

Released:
Source organism: Homo sapiens
Entry authors: Chaikuad A, Savitsky P, Krojer T, Muniz JRC, Filippakopoulos P, Rellos P, Keates T, Fedorov O, Pike ACW, Eswaran J, Berridge G, Phillips C, Zhang Y, von Delft F, Weigelt J, Arrowsmith CH, Edwards AM, Bountra 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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-156012 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 368 amino acids
Theoretical weight: 43.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49760 (Residues: 135-496; Coverage: 73%)
Gene name: CLK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P3221
Unit cell:
a: 97.678Å b: 97.678Å c: 223.029Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.194 0.252
Expression system: Escherichia coli BL21(DE3)