› 5e4a

X-ray diffraction
1.33Å resolution

Human transthyretin (TTR) complexed with (2,7-Dichloro-fluoren-9-ylideneaminooxy)-acetic acid.

Released:
DOI: 10.2210/pdb5e4a/pdb
PDB entry 5e4a coloured by chain, front view.
PDB entry 5e4a coloured by chain, side view.
PDB entry 5e4a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis and structural analysis of halogen substituted fibril formation inhibitors of Human Transthyretin (TTR).
Ciccone L, Nencetti S, Rossello A, Stura EA, Orlandini E
J Enzyme Inhib Med Chem 31 40-51 (2016)
PMID: 27067161

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: 137 amino acids
Theoretical weight: 14.74 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02766 (Residues: 10-146; Coverage: 99%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

1 bound ligand:
Ligand 5JW 1 x 5JW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 43.21Å b: 85.99Å c: 63.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.139 0.192

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)
7 other articles