Fluorine in PDB 7b8t: Levofloxacin Bound Structure of Bacterial Efflux Pump.

The structure of Levofloxacin Bound Structure of Bacterial Efflux Pump., PDB code: 7b8t was solved by J.Wilhelm, H.Sjuts, K.M.Pos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.75 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	108.652, 145.488, 175.156, 90, 90, 90
R / Rfree (%)	22 / 26.9

The binding sites of Fluorine atom in the Levofloxacin Bound Structure of Bacterial Efflux Pump. (pdb code 7b8t). 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 Levofloxacin Bound Structure of Bacterial Efflux Pump., PDB code: 7b8t:

Fluorine binding site 1 out of 1 in the Levofloxacin Bound Structure of Bacterial Efflux Pump.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Levofloxacin Bound Structure of Bacterial Efflux Pump. within 5.0Å range: probe atom residue distance (Å) B Occ C:F901 b:85.4 occ:0.79 F C:LFX901 0.0 85.4 0.8 C11 C:LFX901 1.4 82.3 0.8 C13 C:LFX901 2.3 79.8 0.8 C04 C:LFX901 2.4 85.0 0.8 N01 C:LFX901 2.8 92.0 0.8 C01 C:LFX901 3.2 93.0 0.8 CD2 C:PHE628 3.5 82.1 1.0 C06 C:LFX901 3.6 82.7 0.8 C10 C:LFX901 3.6 78.8 0.8 CE2 C:PHE628 3.6 85.2 1.0 CG2 C:VAL139 3.7 73.5 1.0 C07 C:LFX901 3.9 93.8 0.8 C02 C:LFX901 3.9 92.9 0.8 CG1 C:VAL139 4.0 71.9 1.0 CG C:PHE628 4.0 80.8 1.0 C05 C:LFX901 4.1 80.6 0.8 CZ C:PHE628 4.3 83.9 1.0 CB C:VAL139 4.3 75.3 1.0 CB C:TYR327 4.5 95.0 1.0 C08 C:LFX901 4.5 90.8 0.8 CD1 C:PHE628 4.6 84.6 1.0 CB C:PHE628 4.6 81.8 1.0 CE1 C:PHE628 4.7 83.1 1.0 O01 C:LFX901 4.7 84.8 0.8 CG C:TYR327 4.8 98.5 1.0 C15 C:LFX901 4.8 74.4 0.8 N C:LFX901 4.9 95.1 0.8

A.Ornik-Cha, J.Wilhelm, H.Sjuts, J.Reitz, A.Seybert, A.Frangakis, K.M.Pos. Structural and Functional Analysis of the Promiscuous Acrb and Adeb Efflux Pumps Suggests Different Drug Binding Mechanisms To Be Published.