Sodium in PDB 5o43: 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor.

The structure of 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor., PDB code: 5o43 was solved by N.Bertoletti, A.Heine, F.Braun, G.Klebe, S.Marchais-Oberwinkler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.50
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	91.572, 91.572, 133.090, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 16.7

The structure of 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor. also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Sodium atom in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor. (pdb code 5o43). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor., PDB code: 5o43:

Sodium binding site 1 out of 1 in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Na301 b:18.8 occ:1.00 O A:GLU50 2.3 18.5 0.5 O A:ALA56 2.3 14.7 1.0 O A:GLU50 2.4 17.4 0.5 O A:HOH570 2.4 35.2 1.0 O A:LEU53 2.4 17.5 1.0 O A:HOH474 2.4 36.7 1.0 O A:HOH449 2.5 34.8 1.0 HG3 A:GLU50 2.9 21.6 0.5 H A:ALA56 3.3 18.9 1.0 HA A:PRO54 3.3 21.0 1.0 HG3 A:GLU50 3.3 28.1 0.5 C A:GLU50 3.4 14.7 0.5 C A:GLU50 3.4 14.7 0.5 HA A:GLU50 3.4 16.2 0.5 HG2 A:GLU50 3.4 21.6 0.5 C A:LEU53 3.4 17.1 1.0 HA A:GLU50 3.4 15.7 0.5 C A:ALA56 3.5 16.1 1.0 CG A:GLU50 3.6 18.0 0.5 H A:GLY55 3.7 25.2 1.0 N A:ALA56 3.9 15.8 1.0 CA A:GLU50 3.9 13.5 0.5 CA A:GLU50 3.9 13.1 0.5 CA A:PRO54 4.0 17.5 1.0 N A:PRO54 4.1 18.2 1.0 CG A:GLU50 4.1 23.4 0.5 HB3 A:ALA56 4.1 22.2 1.0 HG2 A:GLU50 4.1 28.1 0.5 H A:LEU53 4.1 19.3 1.0 N A:GLY55 4.1 21.0 1.0 HG12 A:VAL57 4.2 19.7 1.0 CA A:ALA56 4.2 16.7 1.0 HA A:VAL57 4.2 19.9 1.0 CB A:GLU50 4.3 15.2 0.5 C A:PRO54 4.4 22.5 1.0 HB2 A:LEU53 4.5 20.3 1.0 HA A:GLN51 4.5 17.4 1.0 CB A:GLU50 4.5 16.0 0.5 CA A:LEU53 4.5 15.9 1.0 N A:LEU53 4.5 16.1 1.0 N A:GLN51 4.5 13.5 1.0 N A:VAL57 4.6 14.0 1.0 HG13 A:VAL57 4.7 19.7 1.0 CB A:ALA56 4.7 18.5 1.0 CD A:GLU50 4.7 23.1 0.5 HB2 A:GLU50 4.8 18.2 0.5 HB2 A:GLU50 4.8 19.2 0.5 C A:GLY55 4.8 19.4 1.0 CG1 A:VAL57 4.9 16.4 1.0 CA A:GLN51 4.9 14.5 1.0 CA A:VAL57 4.9 16.6 1.0 OE1 A:GLU50 4.9 22.4 0.5 O A:LEU49 5.0 15.7 1.0 C A:GLN51 5.0 15.5 1.0

F.Braun, N.Bertoletti, G.Moller, J.Adamski, M.Frotscher, N.Guragossian, P.A.Madeira Girio, M.Le Borgne, L.Ettouati, P.Falson, S.Muller, G.Vollmer, A.Heine, G.Klebe, S.Marchais-Oberwinkler. Structure-Based Design and Profiling of Novel 17 Beta-HSD14 Inhibitors. Eur J Med Chem V. 155 61 2018.
ISSN: ISSN 1768-3254
PubMed: 29859505
DOI: 10.1016/J.EJMECH.2018.05.029