› 2rsy

Solution NMR

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152371 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase CSK Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.47 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P32577 (Residues: 80-173; Coverage: 21%)
Gene name: Csk
Sequence domains: SH2 domain
Structure domains: SH2 domain
Phosphoprotein associated with glycosphingolipid-enriched microdomains 1 Chain: B
Molecule details ›
Chain: B
Length: 38 amino acids
Theoretical weight: 4.26 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JM80 (Residues: 288-321; Coverage: 8%)
Gene names: Cbp, Pag, Pag1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 90%
Refinement method: simulated annealing, torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

1 review citation

PAG--a multipurpose transmembrane adaptor protein.
Hrdinka et al. (2014)
4 other articles

2 mentions without citation

Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains.
Tanaka et al. (2013)
1 more