› 3vww

X-ray diffraction
1.93Å resolution

Crystal structure of a0-domain of P5 from H. sapiens

Released:
DOI: 10.2210/pdb3vww/pdb
PDB entry 3vww coloured by chain, front view.
PDB entry 3vww coloured by chain, side view.
PDB entry 3vww coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding.
Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K
Sci Rep 3 2456 (2013)
PMID: 23949117

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-172190 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase A6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 116 amino acids
Theoretical weight: 12.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15084 (Residues: 25-140; Coverage: 28%)
Gene names: ERP5, P5, PDIA6, TXNDC7
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
1 modified residue:
Ligand MLY 2 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 90.461Å b: 43.241Å c: 61.245Å
α: 90° β: 101.29° γ: 90°
R-values:
R R work R free
0.176 0.173 0.232
Expression system: Escherichia coli

Quick links

Citations

30 review citations

Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.
Hudson et al. (2015)
29 more

2 mentions without citation

Functions and mechanisms of protein disulfide isomerase family in cancer emergence.
Rahman et al. (2022)
1 more