› 5cn3

X-ray diffraction
1.3Å resolution

X-ray structure of wild-type TTR at 1.30A resolution

Released:
DOI: 10.2210/pdb5cn3/pdb
PDB entry 5cn3 coloured by chain, front view.
PDB entry 5cn3 coloured by chain, side view.
PDB entry 5cn3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses.
Yee AW, Moulin M, Breteau N, Haertlein M, Mitchell EP, Cooper JB, Boeri Erba E, Forsyth VT
OpenAccess logo Angew Chem Int Ed Engl 55 9292-6 (2016)
PMID: 27311939

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: 130 amino acids
Theoretical weight: 14.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 42.751Å b: 85.486Å c: 64.538Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.18
Expression system: Escherichia coli

Quick links

Citations

2 review citations

A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines.
Puglisi et al. (2020)
1 more

7 mentions without citation

Binding of Monovalent and Bivalent Ligands by Transthyretin Causes Different Short- and Long-Distance Conformational Changes.
Corazza et al. (2019)
6 more