PDBe 3grs

X-ray diffraction
1.54Å resolution

REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION

Released:
Source organism: Homo sapiens
Primary publication:
Refined structure of glutathione reductase at 1.54 A resolution.
J. Mol. Biol. 195 701-29 (1987)
PMID: 3656429

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione reductase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 51.64 KDa
Source organism: Homo sapiens
Expression system: Not provided
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
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
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
0.186 0.186 not available
Expression system: Not provided