› 2r9z

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
2 glutathione amide + NAD(+) = glutathione amide disulfide + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione amide reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 463 amino acids
Theoretical weight: 49.21 KDa
Source organism: Marichromatium gracile
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D0VWY5 (Residues: 1-463; Coverage: 100%)
Gene name: garB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand CL 8 x CL
Ligand NI 4 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P41
Unit cell:
a: 71.933Å b: 71.933Å c: 223.854Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.246
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.
Wallen et al. (2008)
3 more

2 mentions without citation

FAD/NADH Dependent Oxidoreductases: From Different Amino Acid Sequences to Similar Protein Shapes for Playing an Ancient Function.
Trisolini et al. (2019)
1 more