X-ray diffraction
1.83Å resolution

Crystal structure of tyrosine-protein kinase SYK with an inhibitor

Source organism: Homo sapiens
Primary publication:
Highly potent and selective pyrazolylpyrimidines as Syk kinase inhibitors.
Bioorg. Med. Chem. Lett. 25 4441-6 (2015)
PMID: 26384287

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Tyrosine-protein kinase SYK Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 33.9 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
  • Canonical: P43405 (Residues: 356-635; Coverage: 44%)
Gene name: SYK
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 39.964Å b: 88.281Å c: 40.85Å
α: 90° β: 91.48° γ: 90°
R R work R free
0.214 0.212 0.249
Expression system: Spodoptera frugiperda