› 4wo0

X-ray diffraction
1.34Å resolution

Crystal structure of transthyretin in complex with apigenin

Released:
DOI: 10.2210/pdb4wo0/pdb
PDB entry 4wo0 coloured by chain, front view.
PDB entry 4wo0 coloured by chain, side view.
PDB entry 4wo0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural evidence for asymmetric ligand binding to transthyretin.
Cianci M, Folli C, Zonta F, Florio P, Berni R, Zanotti G
Acta Crystallogr D Biol Crystallogr 71 1582-92 (2015)
PMID: 26249340

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
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: 127 amino acids
Theoretical weight: 13.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P02766 (Residues: 21-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

1 bound ligand:
Ligand AGI 2 x AGI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21212
Unit cell:
a: 42.66Å b: 85.739Å c: 63.978Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.206
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

2 review citations

Differential Impact of Flavonoids on Redox Modulation, Bioenergetics, and Cell Signaling in Normal and Tumor Cells: A Comprehensive Review.
Kerimi et al. (2018)
1 more

3 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)
2 more