› 1q5m

X-ray diffraction
1.32Å resolution

Binary complex of rabbit 20alpha-hydroxysteroid dehydrogenase with NADPH

Released:
DOI: 10.2210/pdb1q5m/pdb
PDB entry 1q5m coloured by chain, front view.
PDB entry 1q5m coloured by chain, side view.
PDB entry 1q5m coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Loop relaxation, a mechanism that explains the reduced specificity of rabbit 20alpha-hydroxysteroid dehydrogenase, a member of the aldo-keto reductase superfamily.
Couture JF, Legrand P, Cantin L, Labrie F, Luu-The V, Breton R
J Mol Biol 339 89-102 (2004)
PMID: 15123423

Function and Biology Details

Reactions catalysed: 
17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H
(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160419 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin-E(2) 9-reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 36.59 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P80508 (Residues: 2-323; Coverage: 100%)
Gene name: AKR1C5
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 57.54Å b: 85.27Å c: 66.15Å
α: 90° β: 91.48° γ: 90°
R-values:
R R work R free
0.321 0.148 0.177
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Gates of enzymes.
Gora et al. (2013)
20 other articles

7 mentions without citation

Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases.
Lau et al. (2010)
6 more