› 3m31

X-ray diffraction
1.85Å resolution

Structure of the C150A/C295A mutant of S. cerevisiae Ero1p

Released:
DOI: 10.2210/pdb3m31/pdb
PDB entry 3m31 coloured by chain, front view.
PDB entry 3m31 coloured by chain, side view.
PDB entry 3m31 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Steps in reductive activation of the disulfide-generating enzyme Ero1p.
Heldman N, Vonshak O, Sevier CS, Vitu E, Mehlman T, Fass D
Protein Sci 19 1863-76 (2010)
PMID: 20669236

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-169827 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic oxidoreductin-1 Chain: A
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 44.73 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03103 (Residues: 56-424; Coverage: 68%)
Gene names: ERO1, YM4987.05C, YML130C
Sequence domains: Endoplasmic Reticulum Oxidoreductin 1 (ERO1)

Ligands and Environments

3 bound ligands:
Ligand NEN 1 x NEN
Ligand FAD 1 x FAD
Ligand CD 1 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: C2221
Unit cell:
a: 73.441Å b: 132.772Å c: 102.676Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.238
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structure, mechanism, and evolution of Ero1 family enzymes.
Araki et al. (2012)
8 more

1 mention without citation

Steps in reductive activation of the disulfide-generating enzyme Ero1p.
Heldman et al. (2010)