› 2ok7

X-ray diffraction
2.7Å resolution

Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP

Released:
DOI: 10.2210/pdb2ok7/pdb
PDB entry 2ok7 coloured by chain, front view.
PDB entry 2ok7 coloured by chain, side view.
PDB entry 2ok7 coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Ferredoxin-NADP+ reductase from Plasmodium falciparum undergoes NADP+-dependent dimerization and inactivation: functional and crystallographic analysis.
Milani M, Balconi E, Aliverti A, Mastrangelo E, Seeber F, Bolognesi M, Zanetti G
J Mol Biol 367 501-13 (2007)
PMID: 17258767

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111620 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin--NADP reductase, apicoplast Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 316 amino acids
Theoretical weight: 37.32 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: C6KT68 (Residues: 56-371; Coverage: 85%)
Gene names: FNR, PF3D7_0623200
Sequence domains: Oxidoreductase NAD-binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 6 x FAD
2 bound ligands:
Ligand NA 1 x NA
Ligand A2P 6 x A2P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P31
Unit cell:
a: 123.129Å b: 123.129Å c: 133.807Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.263 0.26 0.321
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Structural and functional diversity of ferredoxin-NADP(+) reductases.
Aliverti et al. (2008)
4 more

2 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
1 more