› 5l7y

X-ray diffraction
1.91Å resolution

17beta-hydroxysteroid dehydrogenase 14 variant T205 in complex with a non-steroidal inhibitor.

Released:
DOI: 10.2210/pdb5l7y/pdb
Model geometry
Fit model/data
PDB entry 5l7y coloured by chain, front view.
PDB entry 5l7y coloured by chain, side view.
PDB entry 5l7y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
First Structure-Activity Relationship of 17β-Hydroxysteroid Dehydrogenase Type 14 Nonsteroidal Inhibitors and Crystal Structures in Complex with the Enzyme.
Braun F, Bertoletti N, Möller G, Adamski J, Steinmetzer T, Salah M, Abdelsamie AS, van Koppen CJ, Heine A, Klebe G, Marchais-Oberwinkler S
J Med Chem 59 10719-10737 (2016)
PMID: 27933965

Function and Biology Details

Reaction catalysed: 
A D-threo-aldose + NAD(+) = a D-threo-aldono-1,5-lactone + NADH
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:
L-fucose dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 28.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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
2 bound ligands:
Ligand NA 1 x NA
Ligand 6QO 2 x 6QO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: I422
Unit cell:
a: 91.571Å b: 91.571Å c: 132.518Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.138 0.164
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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