› 2b15

X-ray diffraction
1.7Å resolution

The crystal structure of 2,4-dinitrophenol in complex with human transthyretin

Released:
DOI: 10.2210/pdb2b15/pdb
PDB entry 2b15 coloured by chain, front view.
PDB entry 2b15 coloured by chain, side view.
PDB entry 2b15 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The binding of 2,4-dinitrophenol to wild-type and amyloidogenic transthyretin.
Morais-de-Sá E, Neto-Silva RM, Pereira PJ, Saraiva MJ, Damas AM
Acta Crystallogr D Biol Crystallogr 62 512-9 (2006)
PMID: 16627944

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

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 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

2 bound ligands:
Ligand SO4 2 x SO4
Ligand DNF 2 x DNF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21212
Unit cell:
a: 42.584Å b: 85.612Å c: 63.943Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.218
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

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

15 mentions without citation

Potential role of UGT pharmacogenetics in cancer treatment and prevention: focus on tamoxifen.
Lazarus et al. (2009)
14 more