› 1jeg

Solution NMR

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

Released:
DOI: 10.2210/pdb1jeg/pdb
PDB entry 1jeg coloured by chain, ensemble of 25 models, front view.
PDB entry 1jeg coloured by chain, ensemble of 25 models, side view.
PDB entry 1jeg coloured by chain, ensemble of 25 models, top view.
Source organism: Mus musculus
Primary publication:
A novel, specific interaction involving the Csk SH3 domain and its natural ligand.
Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D
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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151417 (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

Quick links

Citations

23 review citations

Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction.
Li SS. (2005)
22 more

10 mentions without citation

Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.
Kami et al. (2002)
9 more