› 4el1

X-ray diffraction
2.88Å resolution

Crystal structure of oxidized hPDI (abb'xa')

Released:
DOI: 10.2210/pdb4el1/pdb
PDB entry 4el1 coloured by chain, front view.
PDB entry 4el1 coloured by chain, side view.
PDB entry 4el1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase.
Wang C, Li W, Ren J, Fang J, Ke H, Gong W, Feng W, Wang CC
Antioxid Redox Signal 19 36-45 (2013)
PMID: 22657537

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 482 amino acids
Theoretical weight: 54.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07237 (Residues: 18-479; Coverage: 94%)
Gene names: ERBA2L, P4HB, PDI, PDIA1, PO4DB
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 160.748Å b: 34.014Å c: 156.959Å
α: 90° β: 104.89° γ: 90°
R-values:
R R work R free
0.262 0.261 0.282
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Endoplasmic Reticulum Stress and Associated ROS.
Zeeshan et al. (2016)
24 more

34 mentions without citation

Protein disulfide isomerase a multifunctional protein with multiple physiological roles.
Ali Khan et al. (2014)
33 more