› 1a2l

X-ray diffraction
2.7Å resolution

REDUCED DSBA AT 2.7 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1a2l/pdb
PDB entry 1a2l coloured by chain, front view.
PDB entry 1a2l coloured by chain, side view.
PDB entry 1a2l coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.
Guddat LW, Bardwell JC, Martin JL
Structure 6 757-67 (1998)
PMID: 9655827

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbA Chains: A, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 21.16 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEG4 (Residues: 20-208; Coverage: 100%)
Gene names: JW3832, b3860, dsbA, dsf, ppfA
Sequence domains: DSBA-like thioredoxin domain
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21212
Unit cell:
a: 88.88Å b: 83.36Å c: 58.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.285
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.
Hatahet et al. (2009)
20 more

12 mentions without citation

Mechanisms of oxidative protein folding in the bacterial cell envelope.
Kadokura et al. (2010)
11 more