› 3ed3

X-ray diffraction
2Å resolution

Crystal Structure of the Yeast Dithiol/Disulfide Oxidoreductase Mpd1p

Released:
DOI: 10.2210/pdb3ed3/pdb
PDB entry 3ed3 coloured by chain, front view.
PDB entry 3ed3 coloured by chain, side view.
PDB entry 3ed3 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Yeast Mpd1p reveals the structural diversity of the protein disulfide isomerase family.
Vitu E, Gross E, Greenblatt HM, Sevier CS, Kaiser CA, Fass D
J Mol Biol 384 631-40 (2008)
PMID: 18845159

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase MPD1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 34.23 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12404 (Residues: 23-310; Coverage: 97%)
Gene names: MPD1, YOR288C
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand ACT 9 x ACT
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R, ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 48.157Å b: 92.268Å c: 79.337Å
α: 90° β: 92.23° γ: 90°
R-values:
R R work R free
0.219 0.219 0.255
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

6 mentions without citation

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
Fass et al. (2018)
5 more