PDBe 4y9g

X-ray diffraction
1.89Å resolution

Crystal structure of V30M mutated transthyretin in complex with 3-isomangostin

Released:
Source organism: Homo sapiens
Primary publication:
Discovery of γ-Mangostin as an Amyloidogenesis Inhibitor.
OpenAccess logo Sci Rep 5 13570 (2015)
PMID: 26310724

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02766 (Residues: 1-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21212
Unit cell:
a: 43.009Å b: 85.199Å c: 64.462Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.258
Expression system: Escherichia coli