Sodium in PDB 6ffb: 17BETA-Hydroxysteroid Dehydrogenase 14 Variant S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor

The structure of 17BETA-Hydroxysteroid Dehydrogenase 14 Variant S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor, PDB code: 6ffb was solved by N.Bertoletti, A.Heine, G.Klebe, S.Marchais-Oberwinkler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.34 / 1.65
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	91.645, 91.645, 132.555, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 17.5

The structure of 17BETA-Hydroxysteroid Dehydrogenase 14 Variant S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor also contains other interesting chemical elements:

Fluorine

(F)

1 atom

The binding sites of Sodium atom in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor (pdb code 6ffb). 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 S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor, PDB code: 6ffb:

Sodium binding site 1 out of 1 in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant S205 - Mutant Q148A - in Complex with A Nonsteroidal 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 S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Na302 b:21.2 occ:1.00 O A:GLU50 2.3 20.8 0.5 O A:ALA56 2.4 15.7 1.0 O A:HOH572 2.4 40.9 1.0 O A:HOH496 2.4 37.5 1.0 O A:GLU50 2.4 17.4 0.5 O A:HOH547 2.4 35.8 1.0 O A:LEU53 2.4 20.4 1.0 HG3 A:GLU50 2.7 28.9 0.5 H A:ALA56 3.2 18.4 1.0 HA A:PRO54 3.4 23.9 1.0 HG3 A:GLU50 3.4 29.2 0.5 C A:GLU50 3.4 14.4 0.5 C A:GLU50 3.4 15.8 0.5 HA A:GLU50 3.4 18.6 0.5 HA A:GLU50 3.4 19.4 0.5 HG2 A:GLU50 3.4 28.9 0.5 C A:LEU53 3.5 19.3 1.0 CG A:GLU50 3.5 24.1 0.5 C A:ALA56 3.5 16.6 1.0 H A:GLY55 3.8 25.1 1.0 N A:ALA56 3.8 15.3 1.0 CA A:GLU50 3.9 15.5 0.5 CA A:GLU50 3.9 16.1 0.5 CA A:PRO54 4.0 19.9 1.0 HB3 A:ALA56 4.0 23.2 1.0 H A:LEU53 4.1 19.0 1.0 N A:PRO54 4.1 20.9 1.0 N A:GLY55 4.2 21.0 1.0 CG A:GLU50 4.2 24.4 0.5 CA A:ALA56 4.2 15.3 1.0 HA A:VAL57 4.2 21.7 1.0 HG12 A:VAL57 4.2 22.0 1.0 CB A:GLU50 4.3 22.8 0.5 HG2 A:GLU50 4.4 29.2 0.5 C A:PRO54 4.5 22.0 1.0 HA A:GLN51 4.5 21.7 1.0 CB A:GLU50 4.5 23.1 0.5 N A:LEU53 4.5 15.8 1.0 HB2 A:LEU53 4.5 18.1 1.0 CA A:LEU53 4.5 15.3 1.0 N A:GLN51 4.5 17.6 1.0 N A:VAL57 4.6 14.7 1.0 CD A:GLU50 4.6 20.0 0.5 HB2 A:GLU50 4.6 27.7 0.5 CB A:ALA56 4.7 19.3 1.0 HB2 A:GLU50 4.7 27.3 0.5 HG13 A:VAL57 4.7 22.0 1.0 OE2 A:GLU50 4.8 23.8 0.5 C A:GLY55 4.8 22.8 1.0 CA A:VAL57 4.9 18.1 1.0 CA A:GLN51 4.9 18.1 1.0 O A:HOH417 4.9 38.7 1.0 CG1 A:VAL57 4.9 18.4 1.0 O A:LEU49 5.0 20.4 1.0 C A:GLN51 5.0 15.2 1.0

M.J.Badran, N.Bertoletti, A.Keils, A.Heine, G.Klebe, S.Marchais-Oberwinkler. Mutational and Structural Studies Uncover Crucial Amino Acids Determining Activity and Stability of 17 Beta-HSD14. J.Steroid Biochem.Mol.Biol. V. 189 135 2019.
ISSN: ISSN 0960-0760
PubMed: 30836176
DOI: 10.1016/J.JSBMB.2019.02.009