› 3dks

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156483 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thiol:disulfide interchange protein DsbA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 189 amino acids
Theoretical weight: 21.15 KDa
Source organism: Shigella flexneri
Expression system: Escherichia coli
UniProt:
  • Canonical: P52235 (Residues: 20-208; Coverage: 100%)
Gene names: S3816, SF3931, dsbA
Sequence domains: DSBA-like thioredoxin domain
Structure domains: Glutaredoxin
siga peptide Chains: E, F
Molecule details ›
Chains: E, F
Length: 10 amino acids
Theoretical weight: 1.09 KDa
Source organism: Shigella flexneri
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand HSE 2 x HSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 85.433Å b: 87.938Å c: 112.566Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.252
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

9 review citations

How proteins form disulfide bonds.
Depuydt et al. (2011)
8 more

4 mentions without citation

Targeting Bacterial Dsb Proteins for the Development of Anti-Virulence Agents.
Smith et al. (2016)
3 more