› 1grt

X-ray diffraction
2.3Å resolution

HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT

Released:
DOI: 10.2210/pdb1grt/pdb
PDB entry 1grt coloured by chain, front view.
PDB entry 1grt coloured by chain, side view.
PDB entry 1grt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF
Biochemistry 36 6437-47 (1997)
PMID: 9174360

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: 51.72 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
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT
Unit cell:
a: 119.8Å b: 84.5Å c: 63.2Å
α: 90° β: 90° γ: 58.7°
R-values:
R R work R free
0.209 0.209 not available
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Glutathione and its role in cellular functions.
Sies H. (1999)
15 more

2 mentions without citation

Evolution of function in the "two dinucleotide binding domains" flavoproteins.
Ojha et al. (2007)
1 more