› 4p9v

X-ray diffraction
1.64Å resolution

Grb2 SH2 complexed with a pTyr-Ac6cN-Asn tripeptide

Released:
DOI: 10.2210/pdb4p9v/pdb
PDB entry 4p9v coloured by chain, front view.
PDB entry 4p9v coloured by chain, side view.
PDB entry 4p9v coloured by chain, top view.
Source organisms:
Primary publication:
Protein-ligand interactions: probing the energetics of a putative cation-π interaction.
Myslinski JM, Clements JH, Martin SF
Bioorg Med Chem Lett 24 3164-7 (2014)
PMID: 24856058

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158867 (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
PHQ-PTR-02K-ASN-NH2 Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 651 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
2 modified residues:
Ligand PTR 1 x PTR
Ligand 02K 1 x 02K

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 41.935Å b: 41.935Å c: 108.715Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.257
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Amino acid modifications for conformationally constraining naturally occurring and engineered peptide backbones: Insights from the Protein Data Bank.
Di Costanzo et al. (2018)
7 other articles