› 2bmw

X-ray diffraction
1.5Å resolution

Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr, Leu 263 Replaced By Pro, Arg 264 Replaced By Pro and Gly 265 Replaced by Pro (T155G-A160T-L263P-R264P-G265P)

Released:
DOI: 10.2210/pdb2bmw/pdb
PDB entry 2bmw coloured by chain, front view.
PDB entry 2bmw coloured by chain, side view.
PDB entry 2bmw coloured by chain, top view.
Source organism: Nostoc sp. PCC 7119
Primary publication:
Protein motifs involved in coenzyme interaction and enzymatic efficiency in anabaena ferredoxin-NADP+ reductase.
Peregrina JR, Herguedas B, Hermoso JA, Martínez-Júlvez M, Medina M
Biochemistry 48 3109-19 (2009)
PMID: 19219975

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: 304 amino acids
Theoretical weight: 34.12 KDa
Source organism: Nostoc sp. PCC 7119
Expression system: Escherichia coli
UniProt:
  • Canonical: P21890 (Residues: 137-440; 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: ESRF BEAMLINE BM16
Spacegroup: P65
Unit cell:
a: 85.97Å b: 85.97Å c: 96.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.207
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+.
Medina M. (2009)
1 more