PDBe 2zm4

X-ray diffraction
2.7Å resolution

Crystal structure of imidazo quinoxaline 1 bound to the kinase domain of human LCK, activated form (auto-phosphorylated on TYR394)

Released:

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 Lck Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 33.07 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P06239 (Residues: 225-509; Coverage: 56%)
Gene name: LCK
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32B2
Spacegroup: P212121
Unit cell:
a: 42.591Å b: 73.807Å c: 92.159Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.176 0.274
Expression system: Spodoptera frugiperda