› 3c3u

X-ray diffraction
1.8Å resolution

Crystal structure of AKR1C1 in complex with NADP and 3,5-dichlorosalicylic acid

Released:
DOI: 10.2210/pdb3c3u/pdb
PDB entry 3c3u coloured by chain, front view.
PDB entry 3c3u coloured by chain, side view.
PDB entry 3c3u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Selectivity determinants of inhibitor binding to human 20alpha-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid.
Dhagat U, Endo S, Sumii R, Hara A, El-Kabbani O
J Med Chem 51 4844-8 (2008)
PMID: 18620380

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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
2 bound ligands:
Ligand ZN 1 x ZN
Ligand C2U 1 x C2U
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 39.364Å b: 84.236Å c: 49.183Å
α: 90° β: 91.26° γ: 90°
R-values:
R R work R free
0.177 0.174 0.218
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The aldo-keto reductase superfamily and its role in drug metabolism and detoxification.
Barski et al. (2008)
1 more

3 mentions without citation

Integrated bioinformatics and statistical approaches to explore molecular biomarkers for breast cancer diagnosis, prognosis and therapies.
Alam et al. (2022)
2 more