› 1s2c

X-ray diffraction
1.8Å resolution

Crystal structures of prostaglandin D2 11-ketoreductase in complex with the non-steroidal anti-inflammatory drugs flufenamic acid and indomethacin

Released:
DOI: 10.2210/pdb1s2c/pdb
PDB entry 1s2c coloured by chain, front view.
PDB entry 1s2c coloured by chain, side view.
PDB entry 1s2c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of prostaglandin D(2) 11-ketoreductase (AKR1C3) in complex with the nonsteroidal anti-inflammatory drugs flufenamic acid and indomethacin.
Lovering AL, Ride JP, Bunce CM, Desmond JC, Cummings SM, White SA
Cancer Res 64 1802-10 (2004)
PMID: 14996743

Function and Biology Details

Reactions catalysed: 
(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH
5-alpha-androstan-3-beta,17-beta-diol + NADP(+) = 17-beta-hydroxy-5-alpha-androstan-3-one + NADPH
Testosterone + NAD(+) = androstenedione + NADH
A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-oxosteroid + NAD(P)H
Androstan-3-alpha,17-beta-diol + NAD(+) = 17-beta-hydroxyandrostan-3-one + NADH
17-beta-estradiol + NAD(P)(+) = estrone + NAD(P)H
Testosterone + NADP(+) = androst-4-ene-3,17-dione + 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-154612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member C3 Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 37.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P42330 (Residues: 1-323; Coverage: 100%)
Gene names: AKR1C3, DDH1, HSD17B5, KIAA0119, PGFS
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:
Ligand FLF 2 x FLF
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 55.798Å b: 63Å c: 96.289Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.205
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology.
Oppermann U. (2007)
10 more

19 mentions without citation

Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): overview and structural insights.
Byrns et al. (2011)
18 more