PDBe 1jeg

Solution NMR

Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP

Released:
Source organism: Mus musculus
Primary publication:
A novel, specific interaction involving the Csk SH3 domain and its natural ligand.
Nat. Struct. Biol. 8 998-1004 (2001)
PMID: 11685249

Function and Biology Details

Reactions catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase CSK Chain: A
Molecule details ›
Chain: A
Length: 83 amino acids
Theoretical weight: 9.2 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P41241 (Residues: 1-83; Coverage: 18%)
Gene name: Csk
Sequence domains: SH3 domain
Structure domains: SH3 Domains
Tyrosine-protein phosphatase non-receptor type 22 Chain: B
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 2.91 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P29352 (Residues: 605-629; Coverage: 3%)
Gene names: Ptpn22, Ptpn8

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, torsional angle dynmaics
Expression system: Escherichia coli