› 1fvk

X-ray diffraction
1.7Å resolution

THE 1.7 ANGSTROM STRUCTURE OF WILD TYPE DISULFIDE BOND FORMATION PROTEIN (DSBA)

Released:
DOI: 10.2210/pdb1fvk/pdb
PDB entry 1fvk coloured by chain, front view.
PDB entry 1fvk coloured by chain, side view.
PDB entry 1fvk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL
Protein Sci 6 1893-900 (1997)
PMID: 9300489

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142452 (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
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: C2
Unit cell:
a: 117.7Å b: 65.1Å c: 76.4Å
α: 90° β: 126.3° γ: 90°
R-values:
R R work R free
0.198 0.198 0.231

Quick links

Citations

9 review citations

IgG4 breaking the rules.
Aalberse et al. (2002)
8 more

30 mentions without citation

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