3dbq

X-ray diffraction
2.7Å resolution

Crystal structure of TTK kinase domain

Released:
Source organism: Homo sapiens
Primary publication:
Structural and mechanistic insights into Mps1 kinase activation.
J Cell Mol Med 13 1679-1694 (2009)
PMID: 19120698

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

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-152667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase TTK Chain: A
Molecule details ›
Chain: A
Length: 343 amino acids
Theoretical weight: 39.28 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P33981 (Residues: 515-857; Coverage: 40%)
Gene names: MPS1, MPS1L1, TTK
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2221
Unit cell:
a: 105.847Å b: 106.427Å c: 70.682Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.285
Expression system: Spodoptera frugiperda