› 4jic

X-ray diffraction
1.6Å resolution

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 Chains: A, B, C
Molecule details ›
Chains: A, B, C
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 3 x FMN
Ligand PEG 1 x PEG
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 68.446Å b: 93.018Å c: 180.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.19
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

2 mentions 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)
1 more