› 5n5q

X-ray diffraction
2.53Å resolution

Human TTR altered conformation from soaking in iron chloride.

Released:
DOI: 10.2210/pdb5n5q/pdb
PDB entry 5n5q coloured by chain, front view.
PDB entry 5n5q coloured by chain, side view.
PDB entry 5n5q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Copper mediated amyloid-β binding to Transthyretin.
Ciccone L, Fruchart-Gaillard C, Mourier G, Savko M, Nencetti S, Orlandini E, Servent D, Stura EA, Shepard W
Sci Rep 8 13744 (2018)
PMID: 30213975

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: 116 amino acids
Theoretical weight: 12.7 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02766 (Residues: 30-145; Coverage: 91%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family

Ligands and Environments

3 bound ligands:
Ligand ACT 3 x ACT
Ligand FFE 1 x FFE
Ligand FE 5 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21212
Unit cell:
a: 42.73Å b: 81.81Å c: 69.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.192 0.253

Quick links

Citations

10 review citations

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)
9 more

1 mention without citation

Copper mediated amyloid-β binding to Transthyretin.
Ciccone et al. (2018)