Fluorine 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:

Sodium

(Na)

1 atom

The binding sites of Fluorine 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 Fluorine atom.
In total 2 binding sites of Fluorine where determined in the 17BETA-Hydroxysteroid Dehydrogenase 14 Variant T205 in Complex with A Non-Steroidal 2,6-Pyridinketone Inhibitor., PDB code: 5o43:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 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 Fluorine with other atoms in the F 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:F304 b:20.8 occ:1.00 F01 A:9JQ304 0.0 20.8 1.0 C04 A:9JQ304 1.3 15.8 1.0 C03 A:9JQ304 2.3 16.7 1.0 C05 A:9JQ304 2.4 16.6 1.0 HG13 A:VAL143 2.5 21.8 1.0 HG A:SER141 2.7 17.1 1.0 O01 A:9JQ304 2.8 16.5 1.0 OG A:SER141 2.9 14.3 1.0 HA2 A:GLY185 3.2 17.4 1.0 H A:VAL143 3.3 16.1 1.0 CG1 A:VAL143 3.4 18.2 1.0 HG11 A:VAL143 3.5 21.8 1.0 HB3 A:LEU142 3.5 16.6 1.0 C02 A:9JQ304 3.6 19.4 1.0 HG22 A:VAL143 3.6 21.6 1.0 O A:PRO184 3.7 12.4 1.0 C06 A:9JQ304 3.7 15.1 1.0 C5N A:NAD302 3.7 13.8 1.0 H A:LEU142 3.8 15.1 1.0 C4N A:NAD302 3.9 11.2 1.0 HG12 A:VAL143 4.0 21.8 1.0 CA A:GLY185 4.0 14.5 1.0 N A:VAL143 4.0 13.5 1.0 C01 A:9JQ304 4.1 17.6 1.0 C A:GLY185 4.2 17.1 1.0 CB A:SER141 4.2 13.8 1.0 N A:LEU142 4.3 12.6 1.0 CG2 A:VAL143 4.3 18.0 1.0 CB A:VAL143 4.3 16.0 1.0 O A:GLY185 4.3 22.0 1.0 HG21 A:VAL143 4.3 21.6 1.0 HE2 A:TYR154 4.4 14.7 1.0 CB A:LEU142 4.4 13.8 1.0 HB2 A:SER141 4.5 16.6 1.0 C A:PRO184 4.5 13.3 1.0 HE22 A:GLN148 4.6 24.2 1.0 HA A:SER141 4.6 14.0 1.0 HA3 A:GLY185 4.7 17.4 1.0 CA A:LEU142 4.7 12.7 1.0 N A:GLY185 4.8 14.7 1.0 CA A:VAL143 4.8 13.6 1.0 HB3 A:SER141 4.8 16.6 1.0 N A:ASN186 4.8 17.0 1.0 CA A:SER141 4.8 11.7 1.0 C A:LEU142 4.8 13.8 1.0 C6N A:NAD302 4.9 13.8 1.0 HD23 A:LEU142 4.9 18.9 1.0 NE2 A:GLN148 4.9 20.2 1.0 HB2 A:LEU142 4.9 16.6 1.0 C A:SER141 4.9 12.1 1.0 HE21 A:GLN148 5.0 24.2 1.0

Fluorine binding site 2 out of 2 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 Fluorine with other atoms in the F binding site number 2 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:F304 b:32.0 occ:1.00 F02 A:9JQ304 0.0 32.0 1.0 C17 A:9JQ304 1.3 24.8 1.0 C18 A:9JQ304 2.3 24.8 1.0 C16 A:9JQ304 2.4 29.3 1.0 O02 A:9JQ304 2.6 23.2 1.0 C09 A:9JQ304 2.8 25.3 1.0 HE1 A:HIS93 2.8 21.7 1.0 CE1 A:HIS93 3.0 18.1 1.0 N02 A:9JQ304 3.1 24.3 1.0 HG3 A:PRO96 3.3 35.0 1.0 HD13 A:LEU195 3.3 30.6 1.0 NE2 A:HIS93 3.4 16.5 1.0 ND1 A:HIS93 3.5 17.2 1.0 HE2 A:HIS93 3.5 19.8 1.0 C15 A:9JQ304 3.6 27.9 1.0 C13 A:9JQ304 3.6 30.1 1.0 C08 A:9JQ304 3.6 23.3 1.0 HD3 A:PRO96 3.7 35.5 1.0 HD1 A:HIS93 3.8 20.6 1.0 HD22 A:LEU195 4.1 38.3 1.0 C10 A:9JQ304 4.1 22.4 1.0 C14 A:9JQ304 4.1 44.3 1.0 HE22 A:GLN148 4.1 24.2 1.0 CD2 A:HIS93 4.1 15.8 1.0 CG A:PRO96 4.1 29.2 1.0 CG A:HIS93 4.2 14.8 1.0 CD A:PRO96 4.2 29.6 1.0 CD1 A:LEU195 4.3 25.5 1.0 O A:PRO94 4.3 18.2 1.0 HA A:PRO96 4.3 21.3 1.0 NE2 A:GLN148 4.4 20.2 1.0 HD11 A:LEU195 4.4 30.6 1.0 OE1 A:GLN148 4.4 17.2 1.0 N A:PRO96 4.5 19.1 1.0 HB2 A:ALA151 4.5 16.6 1.0 CD A:GLN148 4.5 21.7 1.0 C12 A:9JQ304 4.6 23.1 1.0 O A:HOH486 4.7 16.2 1.0 HB3 A:LEU195 4.7 26.6 1.0 C11 A:9JQ304 4.7 19.6 1.0 HD2 A:HIS93 4.8 18.9 1.0 HG2 A:PRO96 4.8 35.0 1.0 CA A:PRO96 4.8 17.8 1.0 HE21 A:GLN148 4.8 24.2 1.0 HD12 A:LEU195 4.8 30.6 1.0 HA A:PRO95 4.8 23.0 1.0 CD2 A:LEU195 4.8 31.9 1.0 N01 A:9JQ304 4.9 20.9 1.0 HB3 A:PRO96 4.9 28.8 1.0 CB A:PRO96 4.9 24.0 1.0 HD21 A:LEU195 5.0 38.3 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