› 1oo2

X-ray diffraction
1.56Å resolution

Crystal structure of transthyretin from Sparus aurata

Released:
DOI: 10.2210/pdb1oo2/pdb
PDB entry 1oo2 coloured by chain, front view.
PDB entry 1oo2 coloured by chain, side view.
PDB entry 1oo2 coloured by chain, top view.
Source organism: Sparus aurata
Primary publication:
Distinctive binding and structural properties of piscine transthyretin.
Folli C, Pasquato N, Ramazzina I, Battistutta R, Zanotti G, Berni R
FEBS Lett 555 279-84 (2003)
PMID: 14644428

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-192947 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 119 amino acids
Theoretical weight: 12.83 KDa
Source organism: Sparus aurata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9PTT3 (Residues: 33-151; Coverage: 90%)
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2
Unit cell:
a: 96.452Å b: 65.622Å c: 70.834Å
α: 90° β: 97.4° γ: 90°
R-values:
R R work R free
0.203 0.197 0.224
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Disruption of retinoid transport, metabolism and signaling by environmental pollutants.
Novák et al. (2008)
4 more

3 mentions without citation

Predicting the accuracy of protein-ligand docking on homology models.
Bordogna et al. (2011)
2 more