› 3esp

X-ray diffraction
1.31Å resolution

Human transthyretin (TTR) complexed with N-(3,5-Dibromo-4-hydroxyphenyl)-3,5-dimethyl-4-hydroxybenzamide

Released:
DOI: 10.2210/pdb3esp/pdb
PDB entry 3esp coloured by chain, front view.
PDB entry 3esp coloured by chain, side view.
PDB entry 3esp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Toward optimization of the second aryl substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies.
Johnson SM, Connelly S, Wilson IA, Kelly JW
J Med Chem 52 1115-25 (2009)
PMID: 19191553

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: 13.78 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

1 bound ligand:
Ligand DZ3 2 x DZ3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 42.583Å b: 85.337Å c: 64.284Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.201
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.
Johnson et al. (2012)
5 more

2 mentions without citation

Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses.
Connelly et al. (2010)
1 more