› 1bm2

X-ray diffraction
2.1Å resolution

GRB2-SH2 DOMAIN IN COMPLEX WITH CYCLO-[N-ALPHA-ACETYL-L-THI ALYSYL-O-PHOSPHOTYROSYL-VALYL-ASPARAGYL-VALYL-PROLYL] (PKF273-791)

Released:
DOI: 10.2210/pdb1bm2/pdb
PDB entry 1bm2 coloured by chain, front view.
PDB entry 1bm2 coloured by chain, side view.
PDB entry 1bm2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1).
Ettmayer P, France D, Gounarides J, Jarosinski M, Martin MS, Rondeau JM, Sabio M, Topiol S, Weidmann B, Zurini M, Bair KW
J Med Chem 42 971-80 (1999)
PMID: 10090780

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-158853 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Growth factor receptor-bound protein 2 Chain: A
Molecule details ›
Chain: A
Length: 117 amino acids
Theoretical weight: 13.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 49-163; Coverage: 53%)
Gene names: ASH, GRB2
Sequence domains: SH2 domain
Structure domains: SH2 domain
PROTEIN (PKF273-791) Chain: L
Molecule details ›
Chain: L
Length: 7 amino acids
Theoretical weight: 843 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:
Ligand SLZ 1 x SLZ
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: P321
Unit cell:
a: 83.78Å b: 83.78Å c: 31.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.232
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

Correlating structure and energetics in protein-ligand interactions: paradigms and paradoxes.
Martin et al. (2013)
5 more

4 mentions without citation

Insights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions.
Yang et al. (2007)
3 more