› 2rue

Solution NMR

Solution structure of the a' domain of thermophilic fungal protein disulfide (oxidized form, 303K)

Released:
DOI: 10.2210/pdb2rue/pdb
PDB entry 2rue coloured by chain, ensemble of 10 models, front view.
PDB entry 2rue coloured by chain, ensemble of 10 models, side view.
PDB entry 2rue coloured by chain, ensemble of 10 models, top view.
Source organism: Humicola insolens
Primary publication:
Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase.
Inagaki K, Satoh T, Yagi-Utsumi M, Le Gulluche AC, Anzai T, Uekusa Y, Kamiya Y, Kato K
FEBS Lett 589 2690-4 (2015)
PMID: 26272828

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157167 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.12 KDa
Source organism: Humicola insolens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55059 (Residues: 354-469; Coverage: 24%)
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 82%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum.
Soares Moretti et al. (2017)
1 more