› 3lzx

X-ray diffraction
1.9Å resolution

Crystal structure of ferredoxin-NADP+ oxidoreductase from Bacillus subtilis (FORM II)

Released:
DOI: 10.2210/pdb3lzx/pdb
PDB entry 3lzx coloured by chain, front view.
PDB entry 3lzx coloured by chain, side view.
PDB entry 3lzx coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structure analysis of Bacillus subtilis ferredoxin-NADP(+) oxidoreductase and the structural basis for its substrate selectivity.
Komori H, Seo D, Sakurai T, Higuchi Y
Protein Sci 19 2279-90 (2010)
PMID: 20878669

Function and Biology Details

Reaction catalysed: 
2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126472 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin--NADP reductase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 36.88 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O05268 (Residues: 1-332; Coverage: 100%)
Gene names: BSU32110, yumC
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand NAP 2 x NAP
1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: C2
Unit cell:
a: 207.466Å b: 64.85Å c: 61.116Å
α: 90° β: 105.82° γ: 90°
R-values:
R R work R free
0.183 0.181 0.211
Expression system: Escherichia coli

Quick links

Citations

2 review citations

NADPH-generating systems in bacteria and archaea.
Spaans et al. (2015)
1 more

4 mentions without citation

Crystal structure analysis of Bacillus subtilis ferredoxin-NADP(+) oxidoreductase and the structural basis for its substrate selectivity.
Komori et al. (2010)
3 more