› 1ogi

X-ray diffraction
1.64Å resolution

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY AND ALA 160 REPLACED BY THR (T155G-A160T)

Released:
DOI: 10.2210/pdb1ogi/pdb
PDB entry 1ogi coloured by chain, front view.
PDB entry 1ogi coloured by chain, side view.
PDB entry 1ogi coloured by chain, top view.
Source organism: Nostoc sp. PCC 7119
Primary publication:
Involvement of the pyrophosphate and the 2'-phosphate binding regions of ferredoxin-NADP+ reductase in coenzyme specificity.
Tejero J, Martínez-Julvez M, Mayoral T, Luquita A, Sanz-Aparicio J, Hermoso JA, Hurley JK, Tollin G, Gómez-Moreno C, Medina M
J Biol Chem 278 49203-14 (2003)
PMID: 14500716

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: 34.03 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: 87.33Å b: 87.33Å c: 96.558Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.221
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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