› 2qc7

X-ray diffraction
2.9Å resolution

Crystal structure of the protein-disulfide isomerase related chaperone ERp29

Released:
DOI: 10.2210/pdb2qc7/pdb
PDB entry 2qc7 coloured by chain, front view.
PDB entry 2qc7 coloured by chain, side view.
PDB entry 2qc7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29.
Barak NN, Neumann P, Sevvana M, Schutkowski M, Naumann K, Malesević M, Reichardt H, Fischer G, Stubbs MT, Ferrari DM
J Mol Biol 385 1630-42 (2009)
PMID: 19084538

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151611 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum resident protein 29 Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 27.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30040 (Residues: 34-261; Coverage: 100%)
Gene names: C12orf8, ERP28, ERP29
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P2
Unit cell:
a: 58.044Å b: 68.025Å c: 70.088Å
α: 90° β: 107.46° γ: 90°
R-values:
R R work R free
0.265 0.265 0.279
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

3 mentions without citation

The C-terminal domain of ERp29 mediates polyomavirus binding, unfolding, and infection.
Rainey-Barger et al. (2009)
2 more