› 3p82

X-ray diffraction
2.2Å resolution

H184N mutant of pentaerythritol tetranitrate reductase containing bound acetate ion

Released:
DOI: 10.2210/pdb3p82/pdb
PDB entry 3p82 coloured by chain, front view.
PDB entry 3p82 coloured by chain, side view.
PDB entry 3p82 coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
A site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivity.
Toogood HS, Fryszkowska A, Hulley M, Sakuma M, Mansell D, Stephens GM, Gardiner JM, Scrutton NS
Chembiochem 12 738-49 (2011)
PMID: 21374779

Function and Biology Details

Reaction catalysed: 
NADPH + acceptor = NADP(+) + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 39.51 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli
UniProt:
  • Canonical: P71278 (Residues: 1-365; Coverage: 100%)
Gene name: onr
Sequence domains: NADH:flavin oxidoreductase / NADH oxidase family
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P212121
Unit cell:
a: 58.6Å b: 68.899Å c: 85.542Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.144 0.222
Expression system: Escherichia coli

Quick links

Citations

2 review citations

New developments in 'ene'-reductase catalysed biological hydrogenations.
Toogood et al. (2014)
1 more

1 mention without citation

Hepatitis C Virus NS3 Protease and Helicase Inhibitors from Red Sea Sponge (Amphimedon) Species in Green Synthesized Silver Nanoparticles Assisted by in Silico Modeling and Metabolic Profiling.
Shady et al. (2020)