› 5k1n

X-ray diffraction
1.81Å resolution

Human TTR altered by a rhenium tris-carbonyl Pyta-C12 derivative

Released:
DOI: 10.2210/pdb5k1n/pdb
PDB entry 5k1n coloured by chain, front view.
PDB entry 5k1n coloured by chain, side view.
PDB entry 5k1n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human TTR conformation altered by rhenium tris-carbonyl derivatives.
Ciccone L, Policar C, Stura EA, Shepard W
J Struct Biol 195 353-364 (2016)
PMID: 27402536

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: 118 amino acids
Theoretical weight: 12.96 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02766 (Residues: 30-147; Coverage: 93%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

6 bound ligands:
Ligand EDO 2 x EDO
Ligand PEG 1 x PEG
Ligand RE 3 x RE
Ligand ACT 1 x ACT
Ligand DMS 1 x DMS
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21212
Unit cell:
a: 42.65Å b: 82.13Å c: 67.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.224

Quick links

Citations

7 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)
6 more

1 mention without citation

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