› 1gr1

X-ray diffraction
2.5Å resolution

Structure of Ferredoxin-NADP+ Reductase with Glu 139 replaced by Lys (E139K)

Released:
DOI: 10.2210/pdb1gr1/pdb
PDB entry 1gr1 coloured by chain, front view.
PDB entry 1gr1 coloured by chain, side view.
PDB entry 1gr1 coloured by chain, top view.
Source organism: Nostoc sp. PCC 7119
Primary publication:
Probing the role of glutamic acid 139 of Anabaena ferredoxin-NADP+ reductase in the interaction with substrates.
Faro M, Frago S, Mayoral T, Hermoso JA, Sanz-Aparicio J, Gómez-Moreno C, Medina M
Eur J Biochem 269 4938-47 (2002)
PMID: 12383252

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
Expression system: Escherichia coli
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: ENRAF-NONIUS FR571
Spacegroup: P65
Unit cell:
a: 87.03Å b: 87.03Å c: 96.37Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.25
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Open questions in ferredoxin-NADP+ reductase catalytic mechanism.
Carrillo et al. (2003)
2 more

2 mentions without citation

Molecular chaperones and photoreceptor function.
Kosmaoglou et al. (2008)
1 more