PDBe 1nhp

X-ray diffraction
2Å resolution

CRYSTALLOGRAPHIC ANALYSES OF NADH PEROXIDASE CYS42ALA AND CYS42SER MUTANTS: ACTIVE SITE STRUCTURE, MECHANISTIC IMPLICATIONS, AND AN UNUSUAL ENVIRONMENT OF ARG303

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH peroxidase Chain: A
Molecule details ›
Chain: A
Length: 447 amino acids
Theoretical weight: 49.57 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
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 77.6Å b: 134.8Å c: 146.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Not provided