X-ray diffraction
0.95Å resolution

Catalytic cycle of human glutathione reductase near 1 A resolution

Source organism: Homo sapiens
Primary publication:
Catalytic cycle of human glutathione reductase near 1 A resolution.
J. Mol. Biol. 382 371-84 (2008)
PMID: 18638483

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutathione reductase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 51.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • 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
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 120.357Å b: 62.353Å c: 84.035Å
α: 90° β: 122° γ: 90°
R R work R free
0.123 not available 0.152
Expression system: Escherichia coli