6raa

X-ray diffraction
2.1Å resolution

CLK1 Kinase domain with bound imidazopyridin inhibitor TP003

Released:
Source organism: Homo sapiens
Entry authors: Schroeder M, Arrowsmith C, Knapp S, Bountra C, Edwards A, 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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-156010 (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: 39.58 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 91.01Å b: 64.102Å c: 72.383Å
α: 90° β: 117.64° γ: 90°
R-values:
R R work R free
0.19 0.188 0.233
Expression system: Escherichia coli