2iyj

X-ray diffraction
2Å resolution

Crystal structure of the N-terminal dimer domain of E.coli DsbC

Released:
Source organism: Escherichia coli
Primary publication:
Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG.
Acta Crystallogr D Biol Crystallogr 63 465-71 (2007)
PMID: 17372350

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-172145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol:disulfide interchange protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 75 amino acids
Theoretical weight: 7.93 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: Q14F36 (Residues: 3-75; Coverage: 42%)
Gene name: dsbC
Sequence domains: Disulfide bond isomerase protein N-terminus
Structure domains: Disulphide bond isomerase, DsbC/G, N-terminal

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P6522
Unit cell:
a: 42.138Å b: 42.138Å c: 268.677Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.226 0.251