9ez3

X-ray diffraction
2.7Å resolution

Crystal structure of human CLK3 bound to RN129

Released:
Source organism: Homo sapiens
Entry authors: Kraemer A, Raig N, Knapp S

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)
PDBe Complex ID:
PDB-CPX-156013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase CLK3 Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 42.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49761 (Residues: 127-484; Coverage: 73%)
Gene name: CLK3
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41
Unit cell:
a: 74.587Å b: 74.587Å c: 97.035Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.268
Expression system: Escherichia coli