› 3h93

X-ray diffraction
1.5Å resolution

Crystal Structure of Pseudomonas aeruginosa DsbA

Released:
DOI: 10.2210/pdb3h93/pdb
PDB entry 3h93 coloured by chain, front view.
PDB entry 3h93 coloured by chain, side view.
PDB entry 3h93 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Characterization of the DsbA oxidative folding catalyst from Pseudomonas aeruginosa reveals a highly oxidizing protein that binds small molecules.
Shouldice SR, Heras B, Jarrott R, Sharma P, Scanlon MJ, Martin JL
Antioxid Redox Signal 12 921-31 (2010)
PMID: 19788398

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbA Chain: A
Molecule details ›
Chain: A
Length: 192 amino acids
Theoretical weight: 21.65 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C2B2 (Residues: 23-211; Coverage: 100%)
Gene names: PA5489, dsbA
Sequence domains: DSBA-like thioredoxin domain
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand GOL 4 x GOL
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P41
Unit cell:
a: 41.155Å b: 41.155Å c: 98.318Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.112 0.11 0.152
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

8 mentions without citation

Disarming Burkholderia pseudomallei: structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivo.
Ireland et al. (2014)
7 more