› 1wqu

Solution NMR

Solution structure of the human FES SH2 domain

Released:
DOI: 10.2210/pdb1wqu/pdb
PDB entry 1wqu coloured by chain, ensemble of 20 models, front view.
PDB entry 1wqu coloured by chain, ensemble of 20 models, side view.
PDB entry 1wqu coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the Src homology 2 domain from the human feline sarcoma oncogene Fes.
Scott A, Pantoja-Uceda D, Koshiba S, Inoue M, Kigawa T, Terada T, Shirouzu M, Tanaka A, Sugano S, Yokoyama S, Güntert P
J Biomol NMR 31 357-61 (2005)
PMID: 15929003

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-139506 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase Fes/Fps Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.51 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07332 (Residues: 450-550; Coverage: 12%)
Gene names: FES, FPS
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: automated NOESY assignment, torsion angle dynamics, energy minimization
Expression system: Not provided

Quick links

Citations

1 review citation

Automated structure determination from NMR spectra.
Güntert P. (2009)
8 other articles

3 mentions without citation

Objective identification of residue ranges for the superposition of protein structures.
Kirchner et al. (2011)
2 more