Fluorine 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:

Sodium

(Na)

1 atom

The binding sites of Fluorine 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 Fluorine atom.
In total only one binding site of Fluorine was determined in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant S205 - Mutant Q148A - in Complex with A Nonsteroidal Inhibitor, PDB code: 6ffb:

Fluorine 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 Fluorine with other atoms in the F 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:F304 b:25.7 occ:1.00 F A:F45304 0.0 25.7 1.0 C13 A:F45304 1.4 24.3 1.0 C12 A:F45304 2.3 22.2 1.0 C14 A:F45304 2.4 30.6 1.0 HG A:SER141 2.4 27.4 1.0 HG13 A:VAL143 2.7 27.8 1.0 O2 A:F45304 2.8 25.0 1.0 OG A:SER141 2.9 22.9 1.0 HA2 A:GLY185 3.1 20.7 1.0 H A:VAL143 3.5 17.9 1.0 O A:PRO184 3.6 14.9 1.0 HB3 A:LEU142 3.6 19.0 1.0 CG1 A:VAL143 3.6 23.2 1.0 C11 A:F45304 3.6 29.1 1.0 C15 A:F45304 3.6 23.8 1.0 C5N A:NAD301 3.6 16.8 1.0 HG11 A:VAL143 3.7 27.8 1.0 C4N A:NAD301 3.7 13.6 1.0 H A:LEU142 3.8 18.0 1.0 HG22 A:VAL143 3.9 22.2 1.0 CA A:GLY185 4.0 17.3 1.0 C A:GLY185 4.1 15.5 1.0 HG12 A:VAL143 4.1 27.8 1.0 C10 A:F45304 4.1 27.2 1.0 O A:GLY185 4.1 19.9 1.0 N A:VAL143 4.2 14.9 1.0 CB A:SER141 4.3 18.8 1.0 N A:LEU142 4.3 15.0 1.0 HH A:TYR154 4.4 17.7 1.0 C A:PRO184 4.4 14.3 1.0 HB2 A:SER141 4.4 22.6 1.0 CB A:LEU142 4.5 15.8 1.0 HE2 A:TYR154 4.5 19.1 1.0 CG2 A:VAL143 4.5 18.5 1.0 CB A:VAL143 4.6 15.2 1.0 O A:HOH570 4.6 35.7 1.0 HA A:SER141 4.6 17.6 1.0 HG21 A:VAL143 4.6 22.2 1.0 HA3 A:GLY185 4.6 20.7 1.0 N A:GLY185 4.7 17.0 1.0 N A:ASN186 4.8 17.0 1.0 C6N A:NAD301 4.8 15.3 1.0 CA A:LEU142 4.8 13.0 1.0 CA A:SER141 4.9 14.7 1.0 HB2 A:LEU142 4.9 19.0 1.0 HB3 A:SER141 4.9 22.6 1.0 C3N A:NAD301 4.9 12.5 1.0 C A:SER141 5.0 14.9 1.0 HD23 A:LEU142 5.0 24.2 1.0 HA A:ASN186 5.0 15.5 1.0 C A:LEU142 5.0 12.4 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