3uwe

X-ray diffraction
1.68Å resolution

AKR1C3 complexed with 3-phenoxybenzoic acid

Released:
Source organism: Homo sapiens
Primary publication:
Structure of AKR1C3 with 3-phenoxybenzoic acid bound.
Acta Crystallogr Sect F Struct Biol Cryst Commun 68 409-13 (2012)
PMID: 22505408

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 37.99 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:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 58.473Å b: 64.699Å c: 96.959Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.214
Expression system: Escherichia coli