› 3djs

X-ray diffraction
1.8Å resolution

Crystal structure of transthyretin variant L58H at acidic pH

Released:
DOI: 10.2210/pdb3djs/pdb
PDB entry 3djs coloured by chain, front view.
PDB entry 3djs coloured by chain, side view.
PDB entry 3djs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Amyloidogenic potential of transthyretin variants: insights from structural and computational analyses.
Cendron L, Trovato A, Seno F, Folli C, Alfieri B, Zanotti G, Berni R
J Biol Chem 284 25832-41 (2009)
PMID: 19602727

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: 127 amino acids
Theoretical weight: 13.8 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: 43.846Å b: 85.694Å c: 64.478Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.217
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Diagnostic and Treatment Approaches Involving Transthyretin in Amyloidogenic Diseases.
Park et al. (2019)
22 other articles

1 mention without citation

Amyloidogenic potential of transthyretin variants: insights from structural and computational analyses.
Cendron et al. (2009)