PDBe 3a4o

X-ray diffraction
3Å resolution

Lyn kinase domain

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for the inhibitor recognition of human Lyn kinase domain.
Bioorg. Med. Chem. Lett. 19 6557-60 (2009)
PMID: 19857964

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
Macromolecule:
Tyrosine-protein kinase Lyn Chain: X
Molecule details ›
Chain: X
Length: 286 amino acids
Theoretical weight: 32.99 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P07948 (Residues: 233-512; Coverage: 55%)
Gene names: JTK8, LYN
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: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: R3
Unit cell:
a: 128.382Å b: 128.382Å c: 54.875Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.293 0.293 0.324
Expression system: Spodoptera frugiperda