1h42

X-ray diffraction
2.15Å resolution

FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR AND LEU 263 REPLACED BY PRO (T155G-A160T-L263P)

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin--NADP reductase Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 34.14 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P65
Unit cell:
a: 85.81Å b: 85.81Å c: 96.13Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.231
Expression system: Escherichia coli