› 4af6

X-ray diffraction
2.9Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin--NADP reductase, leaf isozyme, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 34.83 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10933 (Residues: 53-360; Coverage: 86%)
Gene name: PETH
Sequence domains: Oxidoreductase NAD-binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: P212121
Unit cell:
a: 73.975Å b: 94.698Å c: 138.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.241 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

A hydrogen bond network in the active site of Anabaena ferredoxin-NADP(+) reductase modulates its catalytic efficiency.
Sánchez-Azqueta et al. (2014)
5 more