PDBe 4yvv

X-ray diffraction
2.3Å resolution

Crystal structure of AKR1C3 complexed with glibenclamide

Released:
Source organism: Homo sapiens
Primary publication:
In vitro inhibition of AKR1Cs by sulphonylureas and the structural basis.
Chem. Biol. Interact. 240 310-315 (2015)
PMID: 26362498

Function and Biology Details

Reactions catalysed:
A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-oxosteroid + NAD(P)H
Testosterone + NAD(+) = androstenedione + NADH
Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H
Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH
(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
Testosterone + NADP(+) = androst-4-ene-3,17-dione + NADPH
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member C3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 36.91 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 2 x NAP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P1
Unit cell:
a: 47.103Å b: 48.973Å c: 83.367Å
α: 74.49° β: 86.64° γ: 69.44°
R-values:
R R work R free
0.201 0.198 0.253
Expression system: Escherichia coli