X-ray diffraction
1.8Å resolution

Crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase in complex with coenzyme NADPH


Function and Biology Details

Reaction catalysed:
Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Aldo-keto reductase family 1 member C21 Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 36.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
  • Canonical: Q91WR5 (Residues: 1-323; Coverage: 100%)
Gene name: Akr1c21
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 84.91Å b: 84.9Å c: 95.83Å
α: 90° β: 90° γ: 90°
R R work R free
0.201 0.198 0.268
Expression system: Escherichia coli