› 4tqh

X-ray diffraction
1.51Å resolution

Human transthyretin (TTR) complexed with 3-(9H-fluoren-9-ylideneaminooxy)ethanoic acid

Released:
DOI: 10.2210/pdb4tqh/pdb
PDB 4tqh coloured by chain and viewed from the front.
PDB 4tqh coloured by chain and viewed from the side.
PDB 4tqh coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
X-ray crystal structure and activity of fluorenyl-based compounds as transthyretin fibrillogenesis inhibitors.
Ciccone L, Nencetti S, Rossello A, Tepshi L, Stura EA, Orlandini E
J Enzyme Inhib Med Chem 1-10 (2015)
PMID: 26235916

Function and Biology Details

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

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: 127 amino acids
Theoretical weight: 13.78 KDa
Source organism: Homo sapiens
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

2 bound ligands:
Ligand ES8 2 x ES8
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 42.44Å b: 85.96Å c: 63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.222

Quick links

Citations

1 review citation

The Positive Side of the Alzheimer's Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1.
Ciccone et al. (2020)
3 other articles