› 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 entry 4tqh coloured by chain, front view.
PDB entry 4tqh coloured by chain, side view.
PDB entry 4tqh coloured by chain, top view.
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 31 824-33 (2016)
PMID: 26235916

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
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)
4 other articles