› 5h0v

X-ray diffraction
1.58Å resolution

Crystal structure of H88A mutated human transthyretin

Released:
DOI: 10.2210/pdb5h0v/pdb
PDB entry 5h0v coloured by chain, front view.
PDB entry 5h0v coloured by chain, side view.
PDB entry 5h0v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stability and crystal structures of His88 mutant human transthyretins.
Yokoyama T, Hanawa Y, Obita T, Mizuguchi M
FEBS Lett 591 1862-1871 (2017)
PMID: 28563699

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 126 amino acids
Theoretical weight: 13.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02766 (Residues: 31-147; Coverage: 92%)
Gene names: PALB, TTR
Sequence domains: HIUase/Transthyretin family

Ligands and Environments

2 bound ligands:
Ligand MPD 2 x MPD
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 64.71Å b: 84.66Å c: 85.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.209
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Transthyretin Misfolding, A Fatal Structural Pathogenesis Mechanism.
Si et al. (2021)
2 other articles

1 mention without citation

High-avidity binding drives nucleation of amyloidogenic transthyretin monomer.
Gao et al. (2022)