4h7x

X-ray diffraction
2.6Å resolution

Crystal structure of the tetratricopeptide repeat (TPR) motif of human dual specificity protein kinase Mps1

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-152667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein kinase TTK Chains: A, B
Molecule details ›
Chains: A, B
Length: 161 amino acids
Theoretical weight: 18.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33981 (Residues: 55-210; Coverage: 18%)
Gene names: MPS1, MPS1L1, TTK
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41212
Unit cell:
a: 79.487Å b: 79.487Å c: 137.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.193 0.24
Expression system: Escherichia coli BL21(DE3)