› 4dht

X-ray diffraction
1.8Å resolution

Small-molecule inhibitors of 14-3-3 protein-protein interactions from virtual screening

Released:
DOI: 10.2210/pdb4dht/pdb
PDB 4dht coloured by chain and viewed from the front.
PDB 4dht coloured by chain and viewed from the side.
PDB 4dht coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 protein-protein interactions.
Thiel P, Röglin L, Meissner N, Hennig S, Kohlbacher O, Ottmann C
Chem. Commun. (Camb.) 49 8468-70 (2013)
PMID: 23939230

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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 BL21(DE3)
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

4 bound ligands:
Ligand MG 2 x MG
Ligand CL 2 x CL
Ligand GOL 1 x GOL
Ligand 0KG 1 x 0KG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 82.32Å b: 112.34Å c: 62.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

14-3-3: A Case Study in PPI Modulation.
Ballone et al. (2018)
6 more

1 mention without citation

Modulators of 14-3-3 Protein-Protein Interactions.
Stevers et al. (2018)