› 3a4e

X-ray diffraction
1.7Å resolution

Crystal structure of Human Transthyretin (E54G)

Released:
DOI: 10.2210/pdb3a4e/pdb
PDB entry 3a4e coloured by chain, front view.
PDB entry 3a4e coloured by chain, side view.
PDB entry 3a4e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of the glutamic acid 54 residue in transthyretin stability and thyroxine binding.
Miyata M, Sato T, Mizuguchi M, Nakamura T, Ikemizu S, Nabeshima Y, Susuki S, Suwa Y, Morioka H, Ando Y, Suico MA, Shuto T, Koga T, Yamagata Y, Kai H
Biochemistry 49 114-23 (2010)
PMID: 19950966

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: 13.71 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

2 bound ligands:
Ligand GOL 3 x GOL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21212
Unit cell:
a: 85.671Å b: 41.617Å c: 63.239Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.238
Expression system: Escherichia coli

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Citations

2 review citations

Evolution of quantitative methods in protein secondary structure determination via deep-ultraviolet resonance Raman spectroscopy.
Roach et al. (2012)
1 more