PDBe 1get

X-ray diffraction
2Å resolution

ANATOMY OF AN ENGINEERED NAD-BINDING SITE

Released:
Source organism: Escherichia coli
Primary publication:
Anatomy of an engineered NAD-binding site.
Protein Sci. 3 1504-14 (1994)
PMID: 7833810

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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 120.5Å b: 74Å c: 60.8Å
α: 90° β: 90° γ: 82.5°
R-values:
R R work R free
0.208 0.208 not available
Expression system: Not provided