› 3boa

X-ray diffraction
3.7Å resolution

Crystal structure of yeast protein disulfide isomerase.

Released:
DOI: 10.2210/pdb3boa/pdb
PDB entry 3boa coloured by chain, front view.
PDB entry 3boa coloured by chain, side view.
PDB entry 3boa coloured by chain, top view.
Source organism: Saccharomyces cerevisiae W303
Primary publication:
The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule.
Tian G, Kober FX, Lewandrowski U, Sickmann A, Lennarz WJ, Schindelin H
J Biol Chem 283 33630-40 (2008)
PMID: 18815132

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148229 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase Chain: A
Molecule details ›
Chain: A
Length: 504 amino acids
Theoretical weight: 56.42 KDa
Source organism: Saccharomyces cerevisiae W303
Expression system: Escherichia coli
UniProt:
  • Canonical: P17967 (Residues: 23-522; Coverage: 100%)
Gene names: MFP1, PDI1, TRG1, YCL043C, YCL313, YCL43C
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: C2221
Unit cell:
a: 116.921Å b: 123.154Å c: 75.721Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.239 0.34
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

12 mentions without citation

Autotaxin: structure-function and signaling.
Perrakis et al. (2014)
11 more