› 4n6j

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171508 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Striatin-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 50 amino acids
Theoretical weight: 6.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13033 (Residues: 86-131; Coverage: 6%)
Gene names: GS2NA, SG2NA, STRN3
Sequence domains: Striatin family
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 1W2B
Spacegroup: P3221
Unit cell:
a: 34.064Å b: 34.064Å c: 161.388Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.204 0.252
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The broken "Off" switch in cancer signaling: PP2A as a regulator of tumorigenesis, drug resistance, and immune surveillance.
Ruvolo PP. (2016)
9 more

3 mentions without citation

Striatins contain a noncanonical coiled coil that binds protein phosphatase 2A A subunit to form a 2:2 heterotetrameric core of striatin-interacting phosphatase and kinase (STRIPAK) complex.
Chen et al. (2014)
2 more