› 1dnc

X-ray diffraction
1.7Å resolution

HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DIGLUTATHIONE-DINITROSO-IRON

Released:
DOI: 10.2210/pdb1dnc/pdb
PDB entry 1dnc coloured by chain, front view.
PDB entry 1dnc coloured by chain, side view.
PDB entry 1dnc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers.
Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA
Nat Struct Biol 5 267-71 (1998)
PMID: 9546215

Function and Biology Details

Reaction catalysed: 
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione reductase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 51.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00390 (Residues: 45-522; Coverage: 92%)
Gene names: GLUR, GRD1, GSR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand GSH 1 x GSH
1 bound ligand:
Ligand PO4 1 x PO4
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 120.08Å b: 63.4Å c: 84.7Å
α: 90° β: 58.33° γ: 90°
R-values:
R R work R free
0.205 0.205 0.248
Expression system: Escherichia coli

Quick links

Citations

29 review citations

Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress.
Klatt et al. (2000)
28 more

2 mentions without citation

Thioredoxin reductase and its inhibitors.
Saccoccia et al. (2014)
1 more