4yvp

X-ray diffraction
2.6Å resolution

Crystal Structure of AKR1C1 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:
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
Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase family 1 member C1 Chains: A, B
Molecule details ›
Chains: A, B
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
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: P21
Unit cell:
a: 49.545Å b: 76.168Å c: 88.706Å
α: 90° β: 94.88° γ: 90°
R-values:
R R work R free
0.213 0.212 0.247
Expression system: Escherichia coli