› 2h5k

X-ray diffraction
3.25Å resolution

Crystal Structure of Complex Between the Domain-Swapped Dimeric Grb2 SH2 Domain and Shc-Derived Ligand, Ac-NH-pTyr-Val-Asn-NH2

Released:
DOI: 10.2210/pdb2h5k/pdb
PDB entry 2h5k coloured by chain, front view.
PDB entry 2h5k coloured by chain, side view.
PDB entry 2h5k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and energetic aspects of Grb2-SH2 domain-swapping.
Benfield AP, Whiddon BB, Clements JH, Martin SF
Arch Biochem Biophys 462 47-53 (2007)
PMID: 17466257

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:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158879 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Growth factor receptor-bound protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 116 amino acids
Theoretical weight: 13.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 53-162; Coverage: 51%)
Gene names: ASH, GRB2
Sequence domains: SH2 domain
Structure domains: SH2 domain
Shc-Derived Ligand Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 498 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CAC 1 x CAC
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6222
Unit cell:
a: 94.859Å b: 94.859Å c: 139.236Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.247 0.3
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

The language of SH2 domain interactions defines phosphotyrosine-mediated signal transduction.
Liu et al. (2012)
4 more

3 mentions without citation

The intertwining of structure and function: proposed helix-swapping of the SH2 domain of Grb7, a regulatory protein implicated in cancer progression and inflammation.
Pias et al. (2010)
2 more