8jp2

X-ray diffraction
1.8Å resolution

Crystal structure of AKR1C1 in complex with DFV

Released:
Source organism: Homo sapiens
Primary publication:
Inhibition of AKR1Cs by liquiritigenin and the structural basis.
Chem Biol Interact 385 110654 (2023)
PMID: 37666442

Function and Biology Details

Reactions catalysed:
Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H
17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)(+) = 17-alpha-hydroxyprogesterone + NAD(P)H
Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H
5-alpha-androstan-3-beta,17-beta-diol + NADP(+) = 17-beta-hydroxy-5-alpha-androstan-3-one + NADPH
A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-oxosteroid + NAD(P)H
Testosterone + NAD(P)(+) = androst-4-ene-3,17-dione + 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
Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-170080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member C1 Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 36.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04828 (Residues: 1-323; Coverage: 100%)
Gene names: AKR1C1, DDH, DDH1
Sequence domains: Aldo/keto reductase family

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 39.462Å b: 83.837Å c: 49.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.249
Expression system: Escherichia coli