› 4jiq

X-ray diffraction
2.49Å resolution

Crystal structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter in complex with 1-nitro-2-phenylpropene

Released:
DOI: 10.2210/pdb4jiq/pdb
PDB entry 4jiq coloured by chain, front view.
PDB entry 4jiq coloured by chain, side view.
PDB entry 4jiq coloured by chain, top view.
Source organism: Agrobacterium tumefaciens
Primary publication:
The structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter reveals the molecular reason for nitro- and ene-reductase activity in OYE homologues.
Oberdorfer G, Binter A, Wallner S, Durchschein K, Hall M, Faber K, Macheroux P, Gruber K
Chembiochem 14 836-45 (2013)
PMID: 23606302

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128277 (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: 377 amino acids
Theoretical weight: 40.57 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O31246 (Residues: 1-371; Coverage: 100%)
Gene name: nerA
Sequence domains: NADH:flavin oxidoreductase / NADH oxidase family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand FMN 1 x FMN
Ligand 1L5 1 x 1L5
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 60.15Å b: 69.98Å c: 91.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.262
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

New developments in 'ene'-reductase catalysed biological hydrogenations.
Toogood et al. (2014)
4 other articles

1 mention without citation

The structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter reveals the molecular reason for nitro- and ene-reductase activity in OYE homologues.
Oberdorfer et al. (2013)