› 1rq1

X-ray diffraction
2.8Å resolution

Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell

Released:
DOI: 10.2210/pdb1rq1/pdb
PDB entry 1rq1 coloured by chain, front view.
PDB entry 1rq1 coloured by chain, side view.
PDB entry 1rq1 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.
Gross E, Kastner DB, Kaiser CA, Fass D
Cell 117 601-10 (2004)
PMID: 15163408

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 386 amino acids
Theoretical weight: 44.45 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03103 (Residues: 55-424; Coverage: 68%)
Gene names: ERO1, YM4987.05C, YML130C
Sequence domains: Endoplasmic Reticulum Oxidoreductin 1 (ERO1)

Ligands and Environments

3 bound ligands:
Ligand CD 2 x CD
Ligand NEN 1 x NEN
Ligand FAD 1 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P62
Unit cell:
a: 106.2Å b: 106.2Å c: 124.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.238
Expression system: Escherichia coli

Quick links

Citations

58 review citations

ER stress and diseases.
Yoshida H. (2007)
57 more

3 mentions without citation

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