› 5oeg

X-ray diffraction
3.15Å resolution

Molecular tweezers modulate 14-3-3 protein-protein interactions

Released:
DOI: 10.2210/pdb5oeg/pdb
PDB entry 5oeg coloured by chain, front view.
PDB entry 5oeg coloured by chain, side view.
PDB entry 5oeg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular tweezers modulate 14-3-3 protein-protein interactions.
Bier D, Rose R, Bravo-Rodriguez K, Bartel M, Ramirez-Anguita JM, Dutt S, Wilch C, Klärner FG, Sanchez-Garcia E, Schrader T, Ottmann C
Nat Chem 5 234-9 (2013)
PMID: 23422566

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152124 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
14-3-3 protein sigma Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 26.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31947 (Residues: 1-231; Coverage: 93%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
Structure domains: 14-3-3 domain

Ligands and Environments

2 bound ligands:
Ligand 9SZ 1 x 9SZ
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C222
Unit cell:
a: 63.5Å b: 154.71Å c: 77.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.181 0.266
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Artificial Molecular Machines.
Erbas-Cakmak et al. (2015)
14 more

2 mentions without citation

14-3-3σ and Its Modulators in Cancer.
Aljabal et al. (2020)
1 more