PDBe 2vag

X-ray diffraction
1.8Å resolution

Crystal structure of di-phosphorylated human CLK1 in complex with a novel substituted indole inhibitor

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK1 Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 39.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49759 (Residues: 148-484; Coverage: 70%)
Gene names: CLK, CLK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 90.95Å b: 64.108Å c: 78.894Å
α: 90° β: 118.17° γ: 90°
R-values:
R R work R free
0.182 0.18 0.225
Expression system: Escherichia coli BL21(DE3)