PDBe 1fyr

X-ray diffraction
2.4Å resolution

DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTAL STRUCTURE OF THE GRB2-SH2 AC-PYVNV COMPLEX

Released:

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

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero octamer
hetero hexamer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Growth factor receptor-bound protein 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 114 amino acids
Theoretical weight: 13.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 50-161; Coverage: 52%)
  • Best match: P62993-2 (Residues: 60-120)
Gene names: ASH, GRB2
Sequence domains: SH2 domain
Structure domains: SHC Adaptor Protein
Hepatocyte growth factor receptor Chains: I, J, K, L
Molecule details ›
Chains: I, J, K, L
Length: 5 amino acids
Theoretical weight: 600 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P08581 (Residues: 1355-1359; Coverage: 0%)
  • Best match: P08581-3 (Residues: 369-371)
Gene name: MET

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P43212
Unit cell:
a: 77.61Å b: 77.61Å c: 183.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.27
Expression systems:
  • Escherichia coli
  • Not provided