PDBe 2dcr

Solution NMR

Fully automated solution structure determination of the Fes SH2 domain

Released:
Source organism: Homo sapiens
Primary publication:
Automated protein structure determination from NMR spectra.
J. Am. Chem. Soc. 128 13112-22 (2006)
PMID: 17017791

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 domain:

Structure analysis Details

Assembly composition:
monomeric (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: Cell free synthesis
UniProt:
  • Canonical: P07332 (Residues: 450-550; Coverage: 12%)
Gene names: FES, FPS
Sequence domains: SH2 domain
Structure domains: SHC Adaptor Protein

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Fully automated NMR spectrum analysis and structure calculation without human intervention. Chemical shift assignments and conformational restraints have not been verified manually.
Expression system: Cell free synthesis