Fluorine in PDB 4f4q: Crystal Structure of M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043

The structure of Crystal Structure of M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043, PDB code: 4f4q was solved by J.Neres, F.Pojer, E.Molteni, L.Chiarelli, G.Riccardi, A.Mattevi, S.T.Cole, C.Binda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.60 / 2.62
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.924, 64.309, 202.841, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 24

The binding sites of Fluorine atom in the Crystal Structure of M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043 (pdb code 4f4q). 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 M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043, PDB code: 4f4q:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043


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 M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:45.4 occ:1.00 FAG A:0SK501 0.0 45.4 1.0 CBG A:0SK501 1.3 46.3 1.0 FAH A:0SK501 2.2 46.3 1.0 FAF A:0SK501 2.2 45.5 1.0 CAW A:0SK501 2.2 46.4 1.0 CAK A:0SK501 2.9 46.4 1.0 CAJ A:0SK501 3.3 46.1 1.0 CD A:LYS374 3.4 24.4 1.0 CB A:LYS374 3.4 24.5 1.0 CG1 A:VAL372 3.7 28.8 1.0 CB A:SER235 3.8 25.8 1.0 CG A:LYS374 4.0 24.2 1.0 CBA A:0SK501 4.2 47.9 1.0 CAX A:0SK501 4.4 46.0 1.0 CG A:LYS141 4.4 28.6 1.0 CA A:LYS141 4.5 25.7 1.0 O A:GLY140 4.6 24.6 1.0 N A:LYS141 4.7 25.1 1.0 CE A:LYS374 4.7 24.0 1.0 C A:GLY140 4.7 24.6 1.0 CA A:SER235 4.8 25.6 1.0 CA A:LYS374 4.8 24.6 1.0 O A:PHE373 4.8 26.2 1.0 CBB A:0SK501 4.8 48.1 1.0 ND2 A:ASN392 4.8 23.3 1.0 OG A:SER235 4.8 26.2 1.0 O A:SER234 4.9 25.8 1.0 CB A:VAL372 4.9 29.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043


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 M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:46.3 occ:1.00 FAH A:0SK501 0.0 46.3 1.0 CBG A:0SK501 1.3 46.3 1.0 FAG A:0SK501 2.2 45.4 1.0 FAF A:0SK501 2.2 45.5 1.0 CAW A:0SK501 2.2 46.4 1.0 CAJ A:0SK501 2.6 46.1 1.0 ND2 A:ASN392 3.3 23.3 1.0 CAK A:0SK501 3.5 46.4 1.0 CD2 A:HIS139 3.6 20.9 1.0 NE2 A:HIS139 3.9 20.9 1.0 CD A:LYS374 3.9 24.4 1.0 CB A:LYS374 3.9 24.5 1.0 CE1 A:PHE376 3.9 22.4 1.0 CAX A:0SK501 4.0 46.0 1.0 CG A:LYS374 4.2 24.2 1.0 CG A:ASN392 4.2 23.4 1.0 CZ A:PHE376 4.3 22.3 1.0 NE2 A:GLN343 4.4 27.5 1.0 O A:GLY140 4.7 24.6 1.0 CBA A:0SK501 4.7 47.9 1.0 NBE A:0SK501 4.8 44.5 1.0 CG1 A:VAL372 4.8 28.8 1.0 CG A:HIS139 4.8 21.2 1.0 CBB A:0SK501 4.8 48.1 1.0 SG A:CYS394 4.9 39.4 1.0 O A:HOH680 4.9 33.6 1.0 CB A:ASN392 4.9 23.6 1.0 OD1 A:ASN392 4.9 23.2 1.0 C A:GLY140 5.0 24.6 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043


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 M. Smegmatis DPRE1 in Complex with Fad and Covalently Bound BTZ043 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:45.5 occ:1.00 FAF A:0SK501 0.0 45.5 1.0 CBG A:0SK501 1.3 46.3 1.0 FAH A:0SK501 2.2 46.3 1.0 FAG A:0SK501 2.2 45.4 1.0 CAW A:0SK501 2.2 46.4 1.0 CAK A:0SK501 2.8 46.4 1.0 C A:GLY140 3.1 24.6 1.0 O A:GLY140 3.3 24.6 1.0 CAJ A:0SK501 3.4 46.1 1.0 N A:LYS141 3.4 25.1 1.0 CA A:GLY140 3.5 23.6 1.0 CD2 A:HIS139 3.8 20.9 1.0 CA A:LYS141 4.0 25.7 1.0 CD A:LYS374 4.0 24.4 1.0 CBA A:0SK501 4.1 47.9 1.0 N A:GLY140 4.2 22.8 1.0 O4 A:FAD502 4.2 25.5 1.0 CG A:LYS141 4.4 28.6 1.0 CAX A:0SK501 4.5 46.0 1.0 NE2 A:HIS139 4.6 20.9 1.0 O A:HIS139 4.6 21.6 1.0 C A:HIS139 4.6 22.3 1.0 CB A:LYS141 4.8 27.0 1.0 OAD A:0SK501 4.8 49.4 1.0 CBB A:0SK501 4.8 48.1 1.0 CE A:LYS374 4.9 24.0 1.0 CG A:HIS139 4.9 21.2 1.0 CAZ A:0SK501 5.0 48.7 1.0 N3 A:FAD502 5.0 25.6 1.0 CG A:LYS374 5.0 24.2 1.0 C4 A:FAD502 5.0 25.5 1.0

J.Neres, F.Pojer, E.Molteni, L.R.Chiarelli, N.Dhar, S.Boy-Rottger, S.Buroni, E.Fullam, G.Degiacomi, A.P.Lucarelli, R.J.Read, G.Zanoni, D.E.Edmondson, E.De Rossi, M.R.Pasca, J.D.Mckinney, P.J.Dyson, G.Riccardi, A.Mattevi, S.T.Cole, C.Binda. Structural Basis For Benzothiazinone-Mediated Killing of Mycobacterium Tuberculosis. Sci Transl Med V. 4 RA121 2012.
ISSN: ISSN 1946-6234
PubMed: 22956199
DOI: 10.1126/SCITRANSLMED.3004395