› 1fhs

Solution NMR

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY DOMAIN-2 OF THE GROWTH FACTOR RECEPTOR BOUND PROTEIN-2, NMR, 18 STRUCTURES

Released:
DOI: 10.2210/pdb1fhs/pdb
PDB entry 1fhs coloured by chain, ensemble of 18 models, front view.
PDB entry 1fhs coloured by chain, ensemble of 18 models, side view.
PDB entry 1fhs coloured by chain, ensemble of 18 models, top view.
Source organism: Homo sapiens
Primary publication:
The three-dimensional solution structure of the SRC homology domain-2 of the growth factor receptor-bound protein-2.
Senior MM, Frederick AF, Black S, Murgolo NJ, Perkins LM, Wilson O, Snow ME, Wang YS
J Biomol NMR 11 153-64 (1998)
PMID: 20700826

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158852 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Growth factor receptor-bound protein 2 Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 53-163; Coverage: 51%)
Gene names: ASH, GRB2
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: DG/SA
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor.
Nioche et al. (2002)
2 more

2 mentions without citation

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