Fluorine in PDB 2xkk: Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate)

The structure of Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate), PDB code: 2xkk was solved by A.Wohlkonig, P.F.Chan, A.P.Fosberry, P.Homes, J.Huang, M.Kranz, V.R.Leydon, T.J.Miles, N.D.Pearson, R.L.Perera, A.J.Shillings, M.N.Gwynn, B.D.Bax, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.17 / 3.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	199.775, 95.566, 118.092, 90.00, 108.27, 90.00
R / Rfree (%)	19.4 / 27

The structure of Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate) also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Fluorine atom in the Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate) (pdb code 2xkk). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate), PDB code: 2xkk:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate)


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 Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate) within 5.0Å range: probe atom residue distance (Å) B Occ E:F1100 b:0.3 occ:1.00 F E:MFX1100 0.0 0.3 1.0 C15 E:MFX1100 1.4 0.9 1.0 C11 E:MFX1100 2.3 0.4 1.0 C17 E:MFX1100 2.4 0.8 1.0 N7 E:DA20 2.5 0.0 1.0 N01 E:MFX1100 2.6 0.8 1.0 C2 E:DT19 2.7 0.6 1.0 N3 E:DT19 2.8 0.5 1.0 O2 E:DT19 2.9 1.0 1.0 C5 E:DA20 3.0 0.9 1.0 C8 E:DA20 3.2 0.2 1.0 N1 E:DT19 3.3 0.1 1.0 C03 E:MFX1100 3.3 0.4 1.0 C6 E:DA20 3.4 99.8 1.0 N6 E:DA20 3.5 0.8 1.0 C4 E:DT19 3.5 0.9 1.0 C14 E:MFX1100 3.6 0.1 1.0 C13 E:MFX1100 3.6 0.2 1.0 C04 E:MFX1100 3.8 0.9 1.0 C4 E:DA20 3.8 0.6 1.0 C6 E:DT19 3.9 0.8 1.0 N9 E:DA20 3.9 0.0 1.0 C5 E:DT19 4.0 0.4 1.0 C1' E:DT19 4.1 0.3 1.0 C2' E:DT19 4.1 0.6 1.0 C12 E:MFX1100 4.1 0.5 1.0 O4 E:DT19 4.2 0.5 1.0 N1 E:DA20 4.5 95.7 1.0 N1 F:DA16 4.6 94.5 1.0 C01 E:MFX1100 4.7 0.7 1.0 O01 E:MFX1100 4.7 0.8 1.0 C19 E:MFX1100 4.8 0.9 1.0 N3 E:DA20 4.9 0.7 1.0 O02 E:MFX1100 4.9 0.5 1.0 C02 E:MFX1100 4.9 0.4 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate)


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 Moxifloxacin, Dna, and A. Baumannii Topo IV (Pare-Parc Fusion Truncate) within 5.0Å range: probe atom residue distance (Å) B Occ F:F1100 b:0.2 occ:1.00 F F:MFX1100 0.0 0.2 1.0 C15 F:MFX1100 1.3 0.7 1.0 C17 F:MFX1100 2.3 0.9 1.0 C11 F:MFX1100 2.4 0.4 1.0 C04 F:MFX1100 2.5 0.5 1.0 N01 F:MFX1100 2.8 0.2 1.0 N7 F:DA20 2.8 1.0 1.0 C8 F:DA20 3.2 0.6 1.0 C2 F:DC19 3.2 0.2 1.0 C5 F:DA20 3.2 0.9 1.0 N3 F:DC19 3.4 0.7 1.0 N1 F:DC19 3.4 0.6 1.0 O2 F:DC19 3.6 0.1 1.0 C14 F:MFX1100 3.6 0.8 1.0 C13 F:MFX1100 3.6 0.2 1.0 C4 F:DC19 3.7 0.2 1.0 N9 F:DA20 3.8 0.7 1.0 C6 F:DC19 3.8 0.7 1.0 C4 F:DA20 3.8 0.4 1.0 C6 F:DA20 3.9 0.3 1.0 C5 F:DC19 4.0 0.5 1.0 C02 F:MFX1100 4.0 0.3 1.0 C2' F:DC19 4.0 0.4 1.0 C12 F:MFX1100 4.1 0.5 1.0 C1' F:DC19 4.1 0.0 1.0 N6 F:DA20 4.1 0.6 1.0 C03 F:MFX1100 4.2 0.6 1.0 N4 F:DC19 4.5 0.0 1.0 O4' F:DA20 4.7 0.4 1.0 N02 F:MFX1100 4.7 0.4 1.0 N1 F:DA20 4.8 0.9 1.0 N3 F:DA20 4.8 0.4 1.0 C19 F:MFX1100 4.8 0.5 1.0 O01 F:MFX1100 4.8 0.1 1.0 C01 F:MFX1100 4.8 0.5 1.0 C1' F:DA20 4.8 0.3 1.0 O02 F:MFX1100 4.9 0.5 1.0 C F:MFX1100 4.9 0.6 1.0

A.Wohlkonig, P.F.Chan, A.P.Fosberry, P.Homes, J.Huang, M.Kranz, V.R.Leydon, T.J.Miles, N.D.Pearson, R.L.Perera, A.J.Shillings, M.N.Gwynn, B.D.Bax. Structural Basis of Quinolone Inhibition of Type Iia Topoisomerases and Target-Mediated Resistance Nat.Struct.Mol.Biol. V. 17 1152 2010.
ISSN: ISSN 1545-9993
PubMed: 20802486
DOI: 10.1038/NSMB.1892