› 4ank

X-ray diffraction
1.7Å resolution

Crystallographic study of novel transthyretin ligands exhibiting negative-cooperativity between two T4 binding sites.

Released:
DOI: 10.2210/pdb4ank/pdb
PDB entry 4ank coloured by chain, front view.
PDB entry 4ank coloured by chain, side view.
PDB entry 4ank coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic study of novel transthyretin ligands exhibiting negative-cooperativity between two thyroxine binding sites.
Tomar D, Khan T, Singh RR, Mishra S, Gupta S, Surolia A, Salunke DM
OpenAccess logo PLoS One 7 e43522 (2012)
PMID: 22973437

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
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: 147 amino acids
Theoretical weight: 15.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02766 (Residues: 1-147; Coverage: 100%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21212
Unit cell:
a: 85.9Å b: 42.57Å c: 64.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.206 0.25
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Transthyretin Stabilization: An Emerging Strategy for the Treatment of Alzheimer's Disease?
Saponaro et al. (2020)
2 more

11 mentions without citation

The ankyrin repeat as molecular architecture for protein recognition.
Mosavi et al. (2004)
10 more