Fluorine in PDB 6zfu: Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066

All present enzymatic activity of Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066:
7.1.1.8;

The structure of Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066, PDB code: 6zfu was solved by K.Amporndanai, P.M.O'neill, W.D.Hong, R.K.Amewu, C.Pidathala, N.G.Berry, G.A.Biagini, S.C.Leung, S.S.Hasnain, S.V.Antonyuk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	89.85 / 3.50
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	210.74, 210.74, 343.935, 90, 90, 120
R / Rfree (%)	22.1 / 23.8

The structure of Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066 also contains other interesting chemical elements:

Iron

(Fe)

5 atoms

The binding sites of Fluorine atom in the Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066 (pdb code 6zfu). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066, PDB code: 6zfu:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066 within 5.0Å range: probe atom residue distance (Å) B Occ C:F408 b:123.2 occ:1.00 F2 C:JHE408 0.0 123.2 1.0 C23 C:JHE408 1.3 121.3 1.0 F C:JHE408 2.1 121.0 1.0 F1 C:JHE408 2.2 132.3 1.0 O2 C:JHE408 2.3 109.0 1.0 C20 C:JHE408 2.9 94.0 1.0 C21 C:JHE408 3.2 88.9 1.0 C19 C:JHE408 4.0 90.6 1.0 C22 C:JHE408 4.4 87.0 1.0 CE C:MET194 4.5 111.1 1.0 CA C:GLY38 4.8 92.3 1.0 CB C:ALA193 4.9 95.5 1.0 CG C:MET194 4.9 104.2 1.0 CG C:MET190 4.9 112.4 1.0 C18 C:JHE408 5.0 86.9 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066 within 5.0Å range: probe atom residue distance (Å) B Occ C:F408 b:121.0 occ:1.00 F C:JHE408 0.0 121.0 1.0 C23 C:JHE408 1.3 121.3 1.0 F2 C:JHE408 2.1 123.2 1.0 F1 C:JHE408 2.2 132.3 1.0 O2 C:JHE408 2.2 109.0 1.0 CG C:MET190 3.3 112.4 1.0 CE C:MET190 3.4 119.9 1.0 C20 C:JHE408 3.5 94.0 1.0 SD C:MET190 3.9 121.5 1.0 CD1 C:ILE42 4.0 94.0 1.0 CD2 C:LEU41 4.2 90.6 1.0 C21 C:JHE408 4.2 88.9 1.0 CB C:MET190 4.3 106.6 1.0 CE C:MET194 4.3 111.1 1.0 CA C:MET190 4.5 101.9 1.0 C19 C:JHE408 4.6 90.6 1.0 CG1 C:ILE42 4.7 94.1 1.0 O C:MET190 4.8 100.3 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Bovine Cytochrome BC1 in Complex with Quinolone Inhibitor RKA066 within 5.0Å range: probe atom residue distance (Å) B Occ C:F408 b:132.3 occ:1.00 F1 C:JHE408 0.0 132.3 1.0 C23 C:JHE408 1.3 121.3 1.0 F2 C:JHE408 2.2 123.2 1.0 F C:JHE408 2.2 121.0 1.0 O2 C:JHE408 2.2 109.0 1.0 C21 C:JHE408 2.8 88.9 1.0 C20 C:JHE408 2.9 94.0 1.0 CE C:MET194 3.3 111.1 1.0 C22 C:JHE408 4.1 87.0 1.0 C19 C:JHE408 4.3 90.6 1.0 CG C:MET190 4.7 112.4 1.0 CD1 C:ILE42 4.8 94.0 1.0 SD C:MET194 4.9 112.6 1.0 CG C:MET194 5.0 104.2 1.0

K.Amporndanai, P.M.O'neill, W.D.Hong, R.K.Amewu, C.Pidathala, N.Berry, G.A.Biangini, S.C.Leung, S.S.Hasnain, S.V.Antonyuk. Targeting the Ubiquinol-Reduction (Qi) Site of the Mitochondrial Cytochrome BC1 Complex For the Development of Next Generation Quinolone Antimalarials To Be Published.