PDBe 2b16

X-ray diffraction
1.75Å resolution

The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant Transthyretin Tyr78Phe

Released:
Source organism: Homo sapiens
Primary publication:
The binding of 2,4-dinitrophenol to wild-type and amyloidogenic transthyretin.
Acta Crystallogr. D Biol. Crystallogr. 62 512-9 (2006)
PMID: 16627944

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 13.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 42.542Å b: 85.869Å c: 63.603Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.236
Expression system: Escherichia coli BL21