› 1ttr

X-ray diffraction
1.9Å resolution

TRANSTHYRETIN-V/122/I CARDIOMYOPATHIC MUTANT

Released:
DOI: 10.2210/pdb1ttr/pdb
PDB entry 1ttr coloured by chain, front view.
PDB entry 1ttr coloured by chain, side view.
PDB entry 1ttr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Val122Ile variant transthyretin - a cardiomyopathic mutant.
Damas AM, Ribeiro S, Lamzin VS, Palha JA, Saraiva MJ
Acta Crystallogr D Biol Crystallogr 52 966-72 (1996)
PMID: 15299606

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-136167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transthyretin Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 13.79 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 43.23Å b: 85.64Å c: 65.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways.
Kelly JW. (1998)
5 more

4 mentions without citation

The supramolecular chemistry of β-sheets.
Cheng et al. (2013)
3 more