› 1gsn

X-ray diffraction
1.7Å resolution

HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE

Released:
DOI: 10.2210/pdb1gsn/pdb
PDB entry 1gsn coloured by chain, front view.
PDB entry 1gsn coloured by chain, side view.
PDB entry 1gsn 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: 51.7 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 GSH 1 x GSH

Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand PO4 1 x PO4
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 119.39Å b: 63.63Å c: 84.72Å
α: 90° β: 58.43° γ: 90°
R-values:
R R work R free
0.207 0.207 0.249
Expression system: Escherichia coli

Quick links

Citations

28 review citations

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

2 mentions without citation

Chemical approaches to detect and analyze protein sulfenic acids.
Furdui et al. (2014)
1 more