› 5n62

X-ray diffraction
1.8Å resolution

Human TTR crystals soaked in manganese chloride.

Released:
DOI: 10.2210/pdb5n62/pdb
PDB entry 5n62 coloured by chain, front view.
PDB entry 5n62 coloured by chain, side view.
PDB entry 5n62 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: 117 amino acids
Theoretical weight: 12.83 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02766 (Residues: 30-146; Coverage: 92%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21212
Unit cell:
a: 43.27Å b: 85.83Å c: 63.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.244

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)