› 1ges

X-ray diffraction
1.74Å resolution

ANATOMY OF AN ENGINEERED NAD-BINDING SITE

Released:
DOI: 10.2210/pdb1ges/pdb
PDB entry 1ges coloured by chain, front view.
PDB entry 1ges coloured by chain, side view.
PDB entry 1ges coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Anatomy of an engineered NAD-binding site.
Mittl PR, Berry A, Scrutton NS, Perham RN, Schulz GE
Protein Sci 3 1504-14 (1994)
PMID: 7833810

Function and Biology Details

Reaction catalysed: 
2 glutathione + NADP(+) = glutathione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139154 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 450 amino acids
Theoretical weight: 48.74 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


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 120Å b: 72.8Å c: 61Å
α: 90° β: 90° γ: 82.8°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Not provided

Quick links

Citations

30 citation in other articles

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.
Brautigam et al. (2005)
29 more

3 mentions without citation

Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems.
Sun et al. (2001)
2 more