X-ray diffraction
2.2Å resolution

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


Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Perakine reductase Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 37.46 KDa
Source organism: Rauvolfia serpentina
Expression system: Escherichia coli
  • 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 58.102Å b: 93.65Å c: 143.077Å
α: 90° β: 90° γ: 90°
R R work R free
0.24 0.212 0.247
Expression system: Escherichia coli