› 5hr3

X-ray diffraction
1.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141959 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 109 amino acids
Theoretical weight: 11.78 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AA25 (Residues: 1-109; Coverage: 100%)
Gene names: JW5856, b3781, fipA, trxA, tsnC
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

3 bound ligands:
Ligand CU 3 x CU
Ligand EOH 2 x EOH
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 29.238Å b: 33.124Å c: 47.185Å
α: 75.75° β: 88.85° γ: 68.83°
R-values:
R R work R free
0.143 0.142 0.163
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The Thioredoxin System of Mammalian Cells and Its Modulators.
Hasan et al. (2022)
2 other articles

3 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
2 more