› 5icm

X-ray diffraction
1.68Å resolution

17beta-hydroxysteroid dehydrogenase type 14 in complex with a non-steroidal inhibitor

Released:
DOI: 10.2210/pdb5icm/pdb
PDB entry 5icm coloured by chain, front view.
PDB entry 5icm coloured by chain, side view.
PDB entry 5icm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
New Insights into Human 17β-Hydroxysteroid Dehydrogenase Type 14: First Crystal Structures in Complex with a Steroidal Ligand and with a Potent Nonsteroidal Inhibitor.
Bertoletti N, Braun F, Lepage M, Möller G, Adamski J, Heine A, Klebe G, Marchais-Oberwinkler S
J Med Chem 59 6961-7 (2016)
PMID: 27362750

Function and Biology Details

Reaction catalysed: 
17-beta-estradiol + NAD(P)(+) = estrone + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
17-beta-hydroxysteroid dehydrogenase 14 Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 28.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9BPX1 (Residues: 1-270; Coverage: 100%)
Gene names: DHRS10, HSD17B14, SDR3, SDR47C1, UNQ502/PRO474
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
3 bound ligands:
Ligand NA 1 x NA
Ligand F45 1 x F45
Ligand GLC 1 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: I422
Unit cell:
a: 91.662Å b: 91.662Å c: 133.909Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.189
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Virtual screening applications in short-chain dehydrogenase/reductase research.
Beck et al. (2017)
1 other article

1 mention without citation

Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.
Mendes et al. (2015)