› 4y9c

X-ray diffraction
1.49Å resolution

Crystal structure of V30M mutated transthyretin with bromide in complex with alpha-mangostin

Released:
DOI: 10.2210/pdb4y9c/pdb
PDB entry 4y9c coloured by chain, front view.
PDB entry 4y9c coloured by chain, side view.
PDB entry 4y9c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of γ-Mangostin as an Amyloidogenesis Inhibitor.
Yokoyama T, Ueda M, Ando Y, Mizuguchi M
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
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136168 (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

2 bound ligands:
Ligand MKS 2 x MKS
Ligand BR 6 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P21212
Unit cell:
a: 43.089Å b: 85.624Å c: 63.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.24
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Inhibition of the Amyloidogenesis of Transthyretin by Natural Products and Synthetic Compounds.
Yokoyama et al. (2018)
1 more

2 mentions without citation

Natural compounds as inhibitors of transthyretin amyloidosis and neuroprotective agents: analysis of structural data for future drug design.
Ciccone et al. (2020)
1 more