› 1qpj

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF THE LYMPHOCYTE-SPECIFIC KINASE LCK IN COMPLEX WITH STAUROSPORINE.

Released:
DOI: 10.2210/pdb1qpj/pdb
PDB entry 1qpj coloured by chain, front view.
PDB entry 1qpj coloured by chain, side view.
PDB entry 1qpj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors.
Zhu X, Kim JL, Newcomb JR, Rose PE, Stover DR, Toledo LM, Zhao H, Morgenstern KA
Structure 7 651-61 (1999)
PMID: 10404594

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: 279 amino acids
Theoretical weight: 32.35 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P06239 (Residues: 231-509; Coverage: 55%)
Gene name: LCK
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand STU 1 x STU
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 61.54Å b: 69.04Å c: 73.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.267
Expression system: Trichoplusia ni

Quick links

Citations

24 review citations

Protein tyrosine kinase structure and function.
Hubbard et al. (2000)
23 more

9 mentions without citation

New horizons in drug discovery of lymphocyte-specific protein tyrosine kinase (Lck) inhibitors: a decade review (2011-2021) focussing on structure-activity relationship (SAR) and docking insights.
Elkamhawy et al. (2021)
8 more