PDBe 1x27

X-ray diffraction
2.7Å resolution

Crystal Structure of Lck SH2-SH3 with SH2 binding site of p130Cas

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

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer anti-estrogen resistance protein 1 Chains: I, J, K, L, M, N
Molecule details ›
Chains: I, J, K, L, M, N
Length: 9 amino acids
Theoretical weight: 1.27 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q63767 (Residues: 759-767; Coverage: 1%)
Gene names: Bcar1, Cas, Crkas
Tyrosine-protein kinase Lck Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 167 amino acids
Theoretical weight: 18.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06239 (Residues: 64-226; Coverage: 32%)
Gene name: LCK
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 77.415Å b: 107.289Å c: 166.389Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.247 0.317
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)