› 5u49

X-ray diffraction
2.22Å resolution

Wild-type Transthyretin in complex with 5-[(1E)-2-(2-Chloro-4-hydroxyphenyl)ethenyl]-1,3-benzenediol

Released:
DOI: 10.2210/pdb5u49/pdb
PDB entry 5u49 coloured by chain, front view.
PDB entry 5u49 coloured by chain, side view.
PDB entry 5u49 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation.
Smith TP, Windsor IW, Forest KT, Raines RT
J Med Chem 60 7820-7834 (2017)
PMID: 28920684

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 Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 13.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02766 (Residues: 21-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family

Ligands and Environments

1 bound ligand:
Ligand S2L 1 x S2L
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: I222
Unit cell:
a: 44.517Å b: 65.895Å c: 84.594Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.202 0.275
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Recent developments in the medicinal chemistry of single boron atom-containing compounds.
Song et al. (2021)
3 more

1 mention without citation

Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation.
Smith et al. (2017)