› 3n8m

X-ray diffraction
2Å resolution

Crystal Structure of the Grb2 SH2 Domain in Complex with An Acyclic Ligand Having the Sequence pYVNVP

Released:
DOI: 10.2210/pdb3n8m/pdb
PDB entry 3n8m coloured by chain, front view.
PDB entry 3n8m coloured by chain, side view.
PDB entry 3n8m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.
Delorbe JE, Clements JH, Whiddon BB, Martin SF
ACS Med Chem Lett 1 448-452 (2010)
PMID: 21116482

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-158861 (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: 13.76 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
PEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 782 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 49.24Å b: 49.24Å c: 86.128Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.224
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 review citations

Counting on natural products for drug design.
Rodrigues et al. (2016)
12 more

3 mentions without citation

Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.
Delorbe et al. (2010)
2 more