5x8i

X-ray diffraction
1.9Å resolution

Crystal structure of human CLK1 in complex with compound 25

Released:

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-156010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 346 amino acids
Theoretical weight: 40.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49759 (Residues: 148-484; Coverage: 70%)
Gene names: CLK, CLK1
Sequence domains: Protein kinase domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P65
Unit cell:
a: 68.33Å b: 68.33Å c: 285.721Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.166 0.206
Expression system: Escherichia coli