4bc6

X-ray diffraction
2.2Å resolution

Crystal structure of human serine threonine kinase-10 bound to novel Bosutinib Isoform 1, previously thought to be Bosutinib

Released:
Source organism: Homo sapiens
Entry authors: Vollmar M, Szklarz M, Chaikuad A, Elkins J, Savitsky P, Azeez KA, Salah E, Krojer T, Canning P, Muniz JRC, Bountra C, Arrowsmith CH, von Delft F, Weigelt J, Edwards A, Knapp S

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase 10 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O94804 (Residues: 24-316; Coverage: 30%)
Gene names: LOK, STK10
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: I222
Unit cell:
a: 51.17Å b: 114.03Å c: 134.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.211 0.254
Expression system: Escherichia coli BL21(DE3)