PDBe 1ger

X-ray diffraction
1.86Å resolution

THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 450 amino acids
Theoretical weight: 48.83 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P06715 (Residues: 1-450; Coverage: 100%)
Gene names: JW3467, b3500, gor
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 120.5Å b: 73.6Å c: 60.5Å
α: 90° β: 90° γ: 83°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Not provided