2npx

X-ray diffraction
2.4Å resolution

NADH BINDING SITE AND CATALYSIS OF NADH PEROXIDASE

Released:
Source organism: Enterococcus faecalis
Primary publication:
NADH binding site and catalysis of NADH peroxidase.
Eur J Biochem 211 221-6 (1993)
PMID: 8425532

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-153337 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH peroxidase Chain: A
Molecule details ›
Chain: A
Length: 447 amino acids
Theoretical weight: 49.65 KDa
Source organism: Enterococcus faecalis
Expression system: Not provided
UniProt:
  • Canonical: P37062 (Residues: 1-447; Coverage: 100%)
Gene names: EF_1211, npr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand NAD 1 x NAD
No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 77.2Å b: 134.5Å c: 145.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 not available
Expression system: Not provided