› 4f9z

X-ray diffraction
2.2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188439 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum resident protein 27 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 227 amino acids
Theoretical weight: 25.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96DN0 (Residues: 30-256; Coverage: 92%)
Gene names: C12orf46, ERP27, UNQ781/PRO1575
Sequence domains: Thioredoxin-like domain
Structure domains: Glutaredoxin

Ligands and Environments

3 bound ligands:
Ligand ACT 13 x ACT
Ligand PE3 1 x PE3
Ligand PE4 1 x PE4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P1
Unit cell:
a: 57.832Å b: 68.359Å c: 86.775Å
α: 70.45° β: 88.16° γ: 64.96°
R-values:
R R work R free
0.171 0.17 0.217
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone.
Wang et al. (2015)
5 more

7 mentions without citation

'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI).
Freedman et al. (2017)
6 more