› 3ove

X-ray diffraction
1.82Å resolution

Crystal Structure of the Grb2 SH2 Domain in Complex with a pYXN-Derived Tripeptide

Released:
DOI: 10.2210/pdb3ove/pdb
PDB entry 3ove coloured by chain, front view.
PDB entry 3ove coloured by chain, side view.
PDB entry 3ove coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Protein-ligand interactions: thermodynamic effects associated with increasing nonpolar surface area.
Myslinski JM, DeLorbe JE, Clements JH, Martin SF
J Am Chem Soc 133 18518-21 (2011)
PMID: 22007755

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-158863 (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: 13.61 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
PYAC7CN Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 554 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 41.935Å b: 41.935Å c: 108.971Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.177 0.26
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

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

1 mention without citation

Protocol for iterative optimization of modified peptides bound to protein targets.
Ochoa et al. (2022)