› 1nhr

X-ray diffraction
2.1Å resolution

AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE IN ENTEROCOCCAL NADH PEROXIDASE TO A DISULFIDE

Released:
DOI: 10.2210/pdb1nhr/pdb
PDB entry 1nhr coloured by chain, front view.
PDB entry 1nhr coloured by chain, side view.
PDB entry 1nhr coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide.
Miller H, Mande SS, Parsonage D, Sarfaty SH, Hol WG, Claiborne A
Biochemistry 34 5180-90 (1995)
PMID: 7711038

Function and Biology Details

Reaction catalysed: 
NADH + H(2)O(2) = NAD(+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

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: 49.59 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:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 77.7Å b: 134.6Å c: 145.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.17 not available
Expression system: Not provided

Quick links

Citations

2 review citations

Protein sulfenic acids in redox signaling.
Poole et al. (2004)
1 more

2 mentions without citation

Evolution of function in the "two dinucleotide binding domains" flavoproteins.
Ojha et al. (2007)
1 more