3v0t

X-ray diffraction
2.33Å resolution

Crystal Structure of Perakine Reductase, Founder Member of a Novel AKR Subfamily with Unique Conformational Changes during NADPH Binding

Released:

Function and Biology Details

Reaction catalysed:
Raucaffrinoline + NADP(+) = perakine + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Perakine reductase Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 37.32 KDa
Source organism: Rauvolfia serpentina
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3L181 (Residues: 1-337; Coverage: 100%)
Gene name: PR
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P3221
Unit cell:
a: 54.501Å b: 54.501Å c: 200.358Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.215 0.254
Expression system: Escherichia coli