› 3ahr

X-ray diffraction
3.07Å resolution

Inactive human Ero1

Released:
DOI: 10.2210/pdb3ahr/pdb
PDB entry 3ahr coloured by chain, front view.
PDB entry 3ahr coloured by chain, side view.
PDB entry 3ahr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI.
Inaba K, Masui S, Iida H, Vavassori S, Sitia R, Suzuki M
EMBO J 29 3330-43 (2010)
PMID: 20834232

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188531 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ERO1-like protein alpha Chain: A
Molecule details ›
Chain: A
Length: 465 amino acids
Theoretical weight: 54.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96HE7 (Residues: 22-468; Coverage: 100%)
Gene names: ERO1A, ERO1L, UNQ434/PRO865
Sequence domains: Endoplasmic Reticulum Oxidoreductin 1 (ERO1)

Ligands and Environments

1 bound ligand:
Ligand FAD 1 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: I222
Unit cell:
a: 54.698Å b: 139.094Å c: 143.491Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.224 0.303
Expression system: Escherichia coli

Quick links

Citations

29 review citations

Protein folding and quality control in the ER.
Araki et al. (2011)
28 more

5 mentions without citation

Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI.
Inaba et al. (2010)
4 more