› 1lkl

X-ray diffraction
1.8Å resolution

HUMAN P56-LCK TYROSINE KINASE SH2 DOMAIN IN COMPLEX WITH THE PHOSPHOTYROSYL PEPTIDE AC-PTYR-GLU-GLU-GLY (PYEEG PEPTIDE)

Released:
DOI: 10.2210/pdb1lkl/pdb
PDB entry 1lkl coloured by chain, front view.
PDB entry 1lkl coloured by chain, side view.
PDB entry 1lkl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution.
Tong L, Warren TC, King J, Betageri R, Rose J, Jakes S
J Mol Biol 256 601-10 (1996)
PMID: 8604142

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 domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138953 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase Lck Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.87 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: SH2 domain
PHOSPHOTYROSYL PEPTIDE AC-PTYR-GLU-GLU-GLY Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 602 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 81.85Å b: 45.15Å c: 26.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Modular peptide recognition domains in eukaryotic signaling.
Kuriyan et al. (1997)
7 more

1 mention without citation

Binding-site assessment by virtual fragment screening.
Huang et al. (2010)