› 1que

X-ray diffraction
1.8Å resolution

X-RAY STRUCTURE OF THE FERREDOXIN:NADP+ REDUCTASE FROM THE CYANOBACTERIUM ANABAENA PCC 7119 AT 1.8 ANGSTROMS

Released:
DOI: 10.2210/pdb1que/pdb
PDB entry 1que coloured by chain, front view.
PDB entry 1que coloured by chain, side view.
PDB entry 1que coloured by chain, top view.
Source organism: Nostoc sp. PCC 7119
Primary publication:
X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolution.
Serre L, Vellieux FM, Medina M, Gomez-Moreno C, Fontecilla-Camps JC, Frey M
J Mol Biol 263 20-39 (1996)
PMID: 8890910

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin--NADP reductase Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 34.04 KDa
Source organism: Nostoc sp. PCC 7119
UniProt:
  • Canonical: P21890 (Residues: 138-440; Coverage: 69%)
Gene name: petH
Sequence domains: Oxidoreductase NAD-binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P65
Unit cell:
a: 88.2Å b: 88.2Å c: 97.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.172 0.214

Quick links

Citations

7 review citations

The evolution, metabolism and functions of the apicoplast.
Lim et al. (2010)
6 more

8 mentions without citation

On the Natural History of Flavin-Based Electron Bifurcation.
Baymann et al. (2018)
7 more