› 1tta

X-ray diffraction
1.7Å resolution

THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1tta/pdb
PDB entry 1tta coloured by chain, front view.
PDB entry 1tta coloured by chain, side view.
PDB entry 1tta coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution.
Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L
J Biol Chem 268 2416-24 (1993)
PMID: 8428915

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: Not provided
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
Spacegroup: P21212
Unit cell:
a: 43.8Å b: 86.22Å c: 65.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 not available not available
Expression system: Not provided

Quick links

Citations

19 review citations

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

20 mentions without citation

Foldamers as versatile frameworks for the design and evolution of function.
Goodman et al. (2007)
19 more