1tjd

X-ray diffraction
2.5Å resolution

The crystal structure of the reduced disulphide bond isomerase, DsbC, from Escherichia coli

Released:
Source organism: Escherichia coli
Primary publication:
Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.
Acta Crystallogr. D Biol. Crystallogr. 60 1747-52 (2004)
PMID: 15388920

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein DsbC Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 23.49 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEG6 (Residues: 21-236; Coverage: 100%)
Gene names: JW2861, b2893, dsbC, xprA
Sequence domains: Thioredoxin-like domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2221
Unit cell:
a: 41.897Å b: 145.799Å c: 73.582Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.203 0.27
Expression system: Escherichia coli