› 2gh5

X-ray diffraction
1.7Å resolution

Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5

Released:
DOI: 10.2210/pdb2gh5/pdb
PDB entry 2gh5 coloured by chain, front view.
PDB entry 2gh5 coloured by chain, side view.
PDB entry 2gh5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme.
Bauer H, Fritz-Wolf K, Winzer A, Kühner S, Little S, Yardley V, Vezin H, Palfey B, Schirmer RH, Davioud-Charvet E
J Am Chem Soc 128 10784-94 (2006)
PMID: 16910673

Function and Biology Details

Reaction catalysed: 
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 478 amino acids
Theoretical weight: 51.64 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 2 x FAD
3 bound ligands:
Ligand PO4 4 x PO4
Ligand ELI 2 x ELI
Ligand GOL 12 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 84.7Å b: 63.6Å c: 103.99Å
α: 90° β: 101.12° γ: 90°
R-values:
R R work R free
0.224 0.224 0.256
Expression system: Escherichia coli

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Citations

6 review citations

Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes.
Deponte M. (2013)
5 more

4 mentions without citation

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