› 2kuq

Solution NMR

Solution structure of the chimera of the PTB domain of SNT-2 and 19-residue peptide (aa 1571-1589) of HALK

Released:
DOI: 10.2210/pdb2kuq/pdb
PDB entry 2kuq coloured by chain, ensemble of 20 models, front view.
PDB entry 2kuq coloured by chain, ensemble of 20 models, side view.
PDB entry 2kuq coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the recognition of nucleophosmin-anaplastic lymphoma kinase oncoprotein by the phosphotyrosine binding domain of Suc1-associated neurotrophic factor-induced tyrosine-phosphorylated target-2.
Koshiba S, Li H, Motoda Y, Tomizawa T, Kasai T, Tochio N, Yabuki T, Harada T, Watanabe S, Tanaka A, Shirouzu M, Kigawa T, Yamamoto T, Yokoyama S
J Struct Funct Genomics 11 125-41 (2010)
PMID: 20454865

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ALK tyrosine kinase receptor; Fibroblast growth factor receptor substrate 3 Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.95 KDa
Source organism: Homo sapiens
Expression system: E. coli-cell-free protein synthesis
UniProt:
  • Canonical: O43559 (Residues: 8-123; Coverage: 24%)
  • Canonical: Q9UM73 (Residues: 1571-1589; Coverage: 1%)
Gene names: ALK, FRS3
Sequence domains: PTB domain (IRS-1 type)
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry
Expression system: E. coli-cell-free protein synthesis

Quick links

Citations

2 review citations

Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.
Ghai et al. (2012)
1 more