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X-ray diffraction
2.7Å resolution

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Lck Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 31.35 KDa
Source organism: Homo sapiens
Expression system: Insect cell
UniProt:
  • Canonical: P06239 (Residues: 231-501; Coverage: 53%)
Gene name: LCK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 979 1 x 979
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 42.1Å b: 73.6Å c: 91.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.264 0.264 0.296
Expression system: Insect cell

Quick links

Citations

4 review citations

Mechanisms of drug resistance in kinases.
Barouch-Bentov et al. (2011)
3 more

1 mention without citation

Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases.
Xu et al. (2015)