Fluorine in PDB 4fdo: Mycobacterium Tuberculosis DPRE1 in Complex with CT319

The structure of Mycobacterium Tuberculosis DPRE1 in Complex with CT319, PDB code: 4fdo was solved by S.M.Batt, G.S.Besra, K.Futterer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.86 / 2.40
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	127.884, 127.884, 64.177, 90.00, 90.00, 120.00
R / Rfree (%)	16.7 / 20.5

The binding sites of Fluorine atom in the Mycobacterium Tuberculosis DPRE1 in Complex with CT319 (pdb code 4fdo). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Mycobacterium Tuberculosis DPRE1 in Complex with CT319, PDB code: 4fdo:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Mycobacterium Tuberculosis DPRE1 in Complex with CT319


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mycobacterium Tuberculosis DPRE1 in Complex with CT319 within 5.0Å range: probe atom residue distance (Å) B Occ A:F901 b:73.3 occ:1.00 F28 A:0T5901 0.0 73.3 1.0 C7 A:0T5901 1.3 69.9 1.0 F27 A:0T5901 2.2 72.5 1.0 F29 A:0T5901 2.2 56.9 1.0 C6 A:0T5901 2.3 64.7 1.0 C1 A:0T5901 2.6 63.1 1.0 N A:LYS134 3.1 20.1 1.0 C A:GLY133 3.2 20.0 1.0 CA A:LYS134 3.5 17.1 1.0 O A:GLY133 3.5 22.1 1.0 C5 A:0T5901 3.6 58.2 1.0 CA A:GLY133 3.8 13.2 1.0 C2 A:0T5901 4.0 61.5 1.0 CB A:LYS134 4.1 18.1 1.0 O4 A:FAD900 4.3 19.1 1.0 CD A:LYS367 4.6 26.7 1.0 N A:GLY133 4.6 18.7 1.0 CB A:SER228 4.7 16.9 1.0 C4 A:0T5901 4.7 56.0 1.0 CD2 A:HIS132 4.7 12.6 1.0 C A:LYS134 4.8 18.0 1.0 O A:HIS132 4.8 13.3 1.0 CG A:LYS134 4.8 28.5 1.0 N8 A:0T5901 4.8 61.7 1.0 C3 A:0T5901 4.9 54.7 1.0 O10 A:0T5901 4.9 69.5 1.0

Fluorine binding site 2 out of 3 in the Mycobacterium Tuberculosis DPRE1 in Complex with CT319


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mycobacterium Tuberculosis DPRE1 in Complex with CT319 within 5.0Å range: probe atom residue distance (Å) B Occ A:F901 b:72.5 occ:1.00 F27 A:0T5901 0.0 72.5 1.0 C7 A:0T5901 1.3 69.9 1.0 F28 A:0T5901 2.2 73.3 1.0 F29 A:0T5901 2.2 56.9 1.0 C6 A:0T5901 2.3 64.7 1.0 C5 A:0T5901 3.1 58.2 1.0 C1 A:0T5901 3.3 63.1 1.0 CB A:SER228 3.7 16.9 1.0 OG A:SER228 3.8 21.8 1.0 CD1 A:LEU317 3.8 50.0 1.0 CB A:LYS134 3.8 18.1 1.0 CA A:LYS134 4.0 17.1 1.0 N A:LYS134 4.1 20.1 1.0 CG A:LYS134 4.2 28.5 1.0 C4 A:0T5901 4.4 56.0 1.0 CG1 A:VAL365 4.4 26.0 1.0 CD A:LYS134 4.4 34.4 1.0 C2 A:0T5901 4.5 61.5 1.0 CE1 A:TYR314 4.7 36.6 1.0 C A:GLY133 4.8 20.0 1.0 O4 A:FAD900 4.9 19.1 1.0 C3 A:0T5901 5.0 54.7 1.0

Fluorine binding site 3 out of 3 in the Mycobacterium Tuberculosis DPRE1 in Complex with CT319


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Mycobacterium Tuberculosis DPRE1 in Complex with CT319 within 5.0Å range: probe atom residue distance (Å) B Occ A:F901 b:56.9 occ:1.00 F29 A:0T5901 0.0 56.9 1.0 C7 A:0T5901 1.3 69.9 1.0 F28 A:0T5901 2.2 73.3 1.0 F27 A:0T5901 2.2 72.5 1.0 C6 A:0T5901 2.3 64.7 1.0 C5 A:0T5901 2.9 58.2 1.0 O4 A:FAD900 3.3 19.1 1.0 N A:LYS134 3.4 20.1 1.0 C1 A:0T5901 3.5 63.1 1.0 CA A:GLY133 3.8 13.2 1.0 C A:GLY133 3.8 20.0 1.0 CE1 A:TYR314 3.9 36.6 1.0 O A:LEU115 3.9 31.9 1.0 N A:GLY117 4.0 16.2 1.0 CA A:LYS134 4.1 17.1 1.0 C A:PRO116 4.1 23.0 1.0 CB A:LYS134 4.2 18.1 1.0 C4 A:0T5901 4.2 56.0 1.0 CA A:PRO116 4.3 21.0 1.0 CD1 A:LEU317 4.5 50.0 1.0 CA A:GLY117 4.5 17.4 1.0 CZ A:TYR314 4.6 38.6 1.0 CD1 A:TYR314 4.6 35.0 1.0 OH A:TYR314 4.6 36.3 1.0 C4 A:FAD900 4.6 16.3 1.0 C2 A:0T5901 4.6 61.5 1.0 O A:HIS132 4.7 13.3 1.0 O A:GLY133 4.7 22.1 1.0 O A:PRO116 4.7 21.8 1.0 C A:LEU115 4.9 24.4 1.0 C3 A:0T5901 4.9 54.7 1.0 N A:GLY133 4.9 18.7 1.0

S.M.Batt, T.Jabeen, V.Bhowruth, L.Quill, P.A.Lund, L.Eggeling, L.J.Alderwick, K.Futterer, G.S.Besra. Structural Basis of Inhibition of Mycobacterium Tuberculosis DPRE1 By Benzothiazinone Inhibitors. Proc.Natl.Acad.Sci.Usa V. 109 11354 2012.
ISSN: ISSN 0027-8424
PubMed: 22733761
DOI: 10.1073/PNAS.1205735109