Fluorine in PDB 8f51: Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine

The structure of Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine, PDB code: 8f51 was solved by A.H.Pang, A.Punetha, S.Garneau-Tsodikova, O.V.Tsodikov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.90 / 2.35
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	175.313, 175.313, 123.308, 90, 90, 120
R / Rfree (%)	16.7 / 20.3

The binding sites of Fluorine atom in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine (pdb code 8f51). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine, PDB code: 8f51:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine


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 Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:52.5 occ:1.00 FAE A:YMZ501 0.0 52.5 1.0 CAZ A:YMZ501 1.3 49.4 1.0 FAF A:YMZ501 2.2 48.7 1.0 FAG A:YMZ501 2.2 53.1 1.0 CAT A:YMZ501 2.3 51.5 1.0 CAI A:YMZ501 2.7 47.7 1.0 CD2 A:LEU63 3.6 24.9 1.0 CAV A:YMZ501 3.6 58.9 1.0 CH2 A:TRP13 3.6 44.5 1.0 CG2 A:VAL40 3.7 28.9 1.0 CZ3 A:TRP13 3.8 47.0 1.0 CA A:ARG37 3.9 50.8 1.0 NAP A:YMZ501 4.1 65.6 1.0 CAH A:YMZ501 4.1 47.3 1.0 N A:ARG37 4.1 49.0 1.0 CB A:ARG37 4.2 57.2 1.0 C A:TRP36 4.4 54.7 1.0 CG A:ARG37 4.4 66.5 1.0 O A:TRP36 4.4 58.6 1.0 CB A:TRP36 4.7 55.8 1.0 CAU A:YMZ501 4.8 61.1 1.0 CB A:VAL40 4.8 29.0 1.0 CZ2 A:TRP13 4.8 44.4 1.0 CD A:ARG37 4.9 65.5 1.0 CG A:LEU63 4.9 24.0 1.0 O A:ALA33 5.0 91.4 1.0 CAJ A:YMZ501 5.0 49.9 1.0

Fluorine binding site 2 out of 6 in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine


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 Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:48.7 occ:1.00 FAF A:YMZ501 0.0 48.7 1.0 CAZ A:YMZ501 1.3 49.4 1.0 FAE A:YMZ501 2.2 52.5 1.0 FAG A:YMZ501 2.2 53.1 1.0 CAT A:YMZ501 2.3 51.5 1.0 NAP A:YMZ501 2.9 65.6 1.0 CAV A:YMZ501 3.0 58.9 1.0 CZ3 A:TRP13 3.2 47.0 1.0 CAI A:YMZ501 3.4 47.7 1.0 CZ A:PHE84 3.4 31.8 1.0 CE2 A:PHE84 3.6 35.3 1.0 CE1 A:PHE84 3.6 35.8 1.0 CH2 A:TRP13 3.8 44.5 1.0 CD2 A:PHE84 3.9 35.9 1.0 CD1 A:PHE84 3.9 34.7 1.0 CE1 A:PHE17 4.0 38.0 1.0 CG A:PHE84 4.0 31.1 1.0 CAR A:YMZ501 4.1 78.0 1.0 CD2 A:LEU63 4.2 24.9 1.0 FAC A:YMZ501 4.2 78.5 1.0 CAU A:YMZ501 4.3 61.1 1.0 CE3 A:TRP13 4.3 47.1 1.0 CAH A:YMZ501 4.6 47.3 1.0 CAY A:YMZ501 4.8 80.9 1.0 CZ A:PHE17 4.8 42.3 1.0 CD1 A:PHE17 4.9 39.9 1.0 CAJ A:YMZ501 4.9 49.9 1.0 CB A:PHE84 5.0 31.5 1.0

Fluorine binding site 3 out of 6 in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine


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 Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:53.1 occ:1.00 FAG A:YMZ501 0.0 53.1 1.0 CAZ A:YMZ501 1.3 49.4 1.0 FAE A:YMZ501 2.2 52.5 1.0 FAF A:YMZ501 2.2 48.7 1.0 CAT A:YMZ501 2.4 51.5 1.0 NAP A:YMZ501 2.7 65.6 1.0 CAV A:YMZ501 2.9 58.9 1.0 O A:ALA33 3.3 91.4 1.0 CAI A:YMZ501 3.5 47.7 1.0 N A:ARG37 3.6 49.0 1.0 CA A:ALA33 3.6 82.0 1.0 CB A:TRP36 3.9 55.8 1.0 CA A:ARG37 3.9 50.8 1.0 C A:ALA33 3.9 79.6 1.0 CB A:ARG37 3.9 57.2 1.0 CAR A:YMZ501 3.9 78.0 1.0 FAC A:YMZ501 4.0 78.5 1.0 CB A:ALA33 4.1 85.4 1.0 C A:TRP36 4.1 54.7 1.0 CAU A:YMZ501 4.2 61.1 1.0 CZ3 A:TRP13 4.4 47.0 1.0 CA A:TRP36 4.5 61.3 1.0 CAY A:YMZ501 4.5 80.9 1.0 CG A:ARG37 4.6 66.5 1.0 CE1 A:PHE17 4.6 38.0 1.0 CAH A:YMZ501 4.7 47.3 1.0 O A:TRP36 4.7 58.6 1.0 CH2 A:TRP13 4.8 44.5 1.0 N A:ALA33 4.8 89.5 1.0 O A:SER32 4.8 76.9 1.0 CD A:ARG37 4.9 65.5 1.0 N A:TRP36 4.9 68.0 1.0 CAJ A:YMZ501 5.0 49.9 1.0

Fluorine binding site 4 out of 6 in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:78.5 occ:1.00 FAC A:YMZ501 0.0 78.5 1.0 CAY A:YMZ501 1.4 80.9 1.0 FAD A:YMZ501 2.2 82.4 1.0 FAB A:YMZ501 2.2 69.4 1.0 CAR A:YMZ501 2.4 78.0 1.0 NAP A:YMZ501 2.7 65.6 1.0 CB A:ALA33 2.8 85.4 1.0 CA A:ALA33 3.2 82.0 1.0 CE1 A:PHE17 3.3 38.0 1.0 N A:ALA33 3.5 89.5 1.0 CD1 A:PHE17 3.7 39.9 1.0 CAK A:YMZ501 3.7 72.3 1.0 FAG A:YMZ501 4.0 53.1 1.0 CAV A:YMZ501 4.1 58.9 1.0 CZ A:PHE17 4.2 42.3 1.0 CE1 A:PHE27 4.2 75.3 1.0 CA A:PRO30 4.2 100.1 1.0 FAF A:YMZ501 4.2 48.7 1.0 O A:GLY29 4.2 103.1 1.0 C A:SER32 4.4 91.5 1.0 CE1 A:PHE84 4.5 35.8 1.0 CZ A:PHE84 4.5 31.8 1.0 C A:GLY29 4.6 102.5 1.0 CAZ A:YMZ501 4.6 49.4 1.0 C A:ALA33 4.6 79.6 1.0 N A:PRO30 4.6 97.1 1.0 CZ A:PHE27 4.6 68.6 1.0 O A:SER32 4.8 76.9 1.0 CG A:PHE17 4.8 40.4 1.0 CAS A:YMZ501 4.8 69.3 1.0 CB A:PRO30 4.8 91.7 1.0 CAT A:YMZ501 4.9 51.5 1.0

Fluorine binding site 5 out of 6 in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:82.4 occ:1.00 FAD A:YMZ501 0.0 82.4 1.0 CAY A:YMZ501 1.4 80.9 1.0 FAC A:YMZ501 2.2 78.5 1.0 FAB A:YMZ501 2.3 69.4 1.0 CAR A:YMZ501 2.3 78.0 1.0 N A:ALA33 2.8 89.5 1.0 CAK A:YMZ501 3.0 72.3 1.0 C A:SER32 3.1 91.5 1.0 CB A:SER32 3.2 90.1 1.0 O A:GLY29 3.3 103.1 1.0 NAP A:YMZ501 3.3 65.6 1.0 CA A:ALA33 3.4 82.0 1.0 CA A:SER32 3.6 88.2 1.0 O A:SER32 3.7 76.9 1.0 CB A:ALA33 3.7 85.4 1.0 N A:SER32 4.0 98.5 1.0 C A:GLY29 4.1 102.5 1.0 OG A:SER32 4.1 75.4 1.0 CAS A:YMZ501 4.3 69.3 1.0 CAV A:YMZ501 4.5 58.9 1.0 CA A:PRO30 4.5 100.1 1.0 CE1 A:PHE27 4.6 75.3 1.0 N A:PRO30 4.7 97.1 1.0 CD1 A:TRP36 4.7 57.9 1.0 N A:GLY29 4.7 109.3 1.0 N A:GLU31 4.7 119.7 1.0 C A:ALA33 4.9 79.6 1.0 CAU A:YMZ501 4.9 61.1 1.0 CA A:GLY29 4.9 104.3 1.0 OAA A:YMZ501 4.9 59.1 1.0

Fluorine binding site 6 out of 6 in the Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Acetyltransferase Eis From M. Tuberculosis in Complex with Mefloquine within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:69.4 occ:1.00 FAB A:YMZ501 0.0 69.4 1.0 CAY A:YMZ501 1.4 80.9 1.0 FAC A:YMZ501 2.2 78.5 1.0 FAD A:YMZ501 2.3 82.4 1.0 CAR A:YMZ501 2.3 78.0 1.0 CE1 A:PHE27 2.5 75.3 1.0 CAK A:YMZ501 2.9 72.3 1.0 CD1 A:PHE27 3.0 73.7 1.0 NAP A:YMZ501 3.3 65.6 1.0 CZ A:PHE27 3.4 68.6 1.0 CE1 A:PHE84 3.9 35.8 1.0 CG A:PHE27 4.2 73.0 1.0 CAS A:YMZ501 4.2 69.3 1.0 O A:GLY29 4.2 103.1 1.0 CZ A:PHE84 4.3 31.8 1.0 CE2 A:PHE27 4.4 73.3 1.0 C A:GLY29 4.5 102.5 1.0 CAV A:YMZ501 4.5 58.9 1.0 CD1 A:PHE17 4.6 39.9 1.0 N A:GLY29 4.7 109.3 1.0 CD2 A:PHE27 4.7 76.7 1.0 CE1 A:PHE17 4.8 38.0 1.0 CA A:GLY29 4.8 104.3 1.0 CAU A:YMZ501 4.8 61.1 1.0 CB A:ALA33 4.9 85.4 1.0 OAA A:YMZ501 4.9 59.1 1.0 N A:ALA33 4.9 89.5 1.0 CB A:ALA20 5.0 29.9 1.0

A.H.Pang, K.D.Green, A.Punetha, N.Thamban Chandrika, K.C.Howard, S.Garneau-Tsodikova, O.V.Tsodikov. Discovery and Mechanistic Analysis of Structurally Diverse Inhibitors of Acetyltransferase Eis Among Fda-Approved Drugs. Biochemistry 2023.
ISSN: ISSN 0006-2960
PubMed: 36657084
DOI: 10.1021/ACS.BIOCHEM.2C00658