PDBe 1fbz

X-ray diffraction
2.4Å resolution

Structure-based design of a novel, osteoclast-selective, nonpeptide Src SH2 inhibitor with in vivo anti-resorptive activity

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Lck Chains: A, B
Molecule details ›
Chains: A, B
Length: 104 amino acids
Theoretical weight: 11.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06239 (Residues: 123-226; Coverage: 20%)
Gene name: LCK
Sequence domains: SH2 domain
Structure domains: SHC Adaptor Protein

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 44.87Å b: 56.26Å c: 102.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.36
Expression system: Escherichia coli