› 5grt

X-ray diffraction
2.4Å resolution

HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, GLUTATHIONYLSPERMIDINE COMPLEX

Released:
DOI: 10.2210/pdb5grt/pdb
PDB entry 5grt coloured by chain, front view.
PDB entry 5grt coloured by chain, side view.
PDB entry 5grt 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:
  • not assigned
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: 461 amino acids
Theoretical weight: 50.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00390 (Residues: 62-522; Coverage: 88%)
Gene names: GLUR, GRD1, GSR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand TS4 1 x TS4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-18
Unit cell:
a: 120.12Å b: 84.79Å c: 63.65Å
α: 90° β: 90° γ: 58.41°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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