Sodium in PDB 5o42: 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: 5o42 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)	37.69 / 1.76
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	91.461, 91.461, 133.087, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 19.1

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 5o42). 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: 5o42:

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:Na302 b:21.5 occ:1.00 O A:GLU50 2.3 16.9 0.6 O A:LEU53 2.4 19.1 1.0 O A:ALA56 2.4 17.6 1.0 O A:GLU50 2.4 18.0 0.5 O A:HOH513 2.4 42.6 1.0 O A:HOH554 2.5 40.4 1.0 O A:HOH418 2.5 31.2 1.0 HG3 A:GLU50 2.9 25.4 0.5 H A:ALA56 3.3 19.1 1.0 HA A:PRO54 3.3 26.9 1.0 HG2 A:GLU50 3.3 25.4 0.5 C A:LEU53 3.4 19.9 1.0 HA A:GLU50 3.4 21.0 0.5 C A:GLU50 3.4 19.7 0.6 C A:GLU50 3.4 18.9 0.5 HA A:GLU50 3.4 21.4 0.6 HG3 A:GLU50 3.5 28.0 0.6 CG A:GLU50 3.5 21.2 0.5 C A:ALA56 3.6 18.1 1.0 H A:GLY55 3.7 29.9 1.0 CA A:GLU50 3.9 17.5 0.5 N A:ALA56 3.9 15.9 1.0 CA A:GLU50 3.9 17.8 0.6 CA A:PRO54 4.0 22.5 1.0 H A:LEU53 4.0 19.6 1.0 N A:PRO54 4.0 20.6 1.0 HB3 A:ALA56 4.1 23.3 1.0 N A:GLY55 4.1 24.9 1.0 HG12 A:VAL57 4.1 22.5 1.0 CA A:ALA56 4.2 17.0 1.0 HA A:VAL57 4.3 20.4 1.0 CG A:GLU50 4.3 23.3 0.6 CB A:GLU50 4.3 17.8 0.5 C A:PRO54 4.4 20.2 1.0 N A:LEU53 4.4 16.3 1.0 HB2 A:LEU53 4.4 19.3 1.0 CA A:LEU53 4.5 15.9 1.0 HA A:GLN51 4.5 20.3 1.0 CB A:GLU50 4.5 19.8 0.6 N A:GLN51 4.6 16.0 1.0 HB2 A:GLU50 4.6 23.7 0.6 HG2 A:GLU50 4.6 28.0 0.6 N A:VAL57 4.6 17.2 1.0 HG13 A:VAL57 4.7 22.5 1.0 CB A:ALA56 4.7 19.4 1.0 CD A:GLU50 4.7 21.5 0.5 HB2 A:GLU50 4.8 21.4 0.5 CG1 A:VAL57 4.9 18.7 1.0 C A:GLY55 4.9 21.7 1.0 OE1 A:GLU50 4.9 21.9 0.5 CA A:GLN51 4.9 16.9 1.0 CA A:VAL57 4.9 17.0 1.0 O A:LEU49 4.9 19.8 1.0 C A:GLN51 4.9 19.1 1.0 CB A:LEU53 5.0 16.1 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