Fluorine in PDB 5bns: E. Coli Fabh with Small Molecule Inhibitor 2

All present enzymatic activity of E. Coli Fabh with Small Molecule Inhibitor 2:
2.3.1.180;

The structure of E. Coli Fabh with Small Molecule Inhibitor 2, PDB code: 5bns was solved by S.L.Kazmirski, D.C.Mckinney, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.34 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.907, 66.878, 162.011, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 28.7

The binding sites of Fluorine atom in the E. Coli Fabh with Small Molecule Inhibitor 2 (pdb code 5bns). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the E. Coli Fabh with Small Molecule Inhibitor 2, PDB code: 5bns:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the E. Coli Fabh with Small Molecule Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of E. Coli Fabh with Small Molecule Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:37.2 occ:1.00 F A:4VM401 0.0 37.2 1.0 C26 A:4VM401 1.3 33.9 1.0 C25 A:4VM401 2.3 29.7 1.0 C21 A:4VM401 2.4 34.9 1.0 CD1 A:ILE250 2.7 34.7 1.0 C19 A:4VM401 2.9 33.2 1.0 C20 A:4VM401 3.0 36.1 1.0 CB A:ALA216 3.4 34.7 1.0 C24 A:4VM401 3.6 31.0 1.0 C22 A:4VM401 3.6 33.3 1.0 CG1 A:VAL212 3.7 38.0 1.0 CA A:PHE213 3.8 35.1 1.0 N A:PHE213 4.0 36.0 1.0 C18 A:4VM401 4.0 34.3 1.0 C23 A:4VM401 4.1 33.4 1.0 C A:VAL212 4.1 39.3 1.0 O A:VAL212 4.1 38.7 1.0 N3 A:4VM401 4.1 35.7 1.0 CG1 A:ILE250 4.2 38.8 1.0 CB A:ALA246 4.5 34.6 1.0 CB A:VAL212 4.6 38.3 1.0 CB A:PHE213 4.7 35.8 1.0 O A:PHE213 4.8 38.9 1.0 C A:PHE213 4.8 39.5 1.0 CA A:ALA216 4.9 34.7 1.0 C17 A:4VM401 4.9 35.5 1.0 C16 A:4VM401 4.9 35.7 1.0

Fluorine binding site 2 out of 2 in the E. Coli Fabh with Small Molecule Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of E. Coli Fabh with Small Molecule Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:49.0 occ:1.00 F B:4VM401 0.0 49.0 1.0 C26 B:4VM401 1.3 43.6 1.0 C25 B:4VM401 2.3 40.0 1.0 C21 B:4VM401 2.4 42.5 1.0 CD1 B:ILE250 2.8 42.6 1.0 C19 B:4VM401 2.9 43.3 1.0 C18 B:4VM401 3.0 41.8 1.0 CB B:ALA216 3.1 35.9 1.0 C24 B:4VM401 3.6 39.7 1.0 C22 B:4VM401 3.6 38.7 1.0 CG1 B:VAL212 3.7 34.6 1.0 CG1 B:ILE250 4.0 37.9 1.0 C20 B:4VM401 4.1 44.2 1.0 C23 B:4VM401 4.1 40.0 1.0 C17 B:4VM401 4.2 41.4 1.0 O B:VAL212 4.3 43.3 1.0 CA B:PHE213 4.3 37.2 1.0 C B:VAL212 4.4 42.1 1.0 CB B:ALA246 4.4 38.4 1.0 N B:PHE213 4.4 38.1 1.0 CG2 B:ILE250 4.6 35.3 1.0 CA B:ALA216 4.7 35.7 1.0 CB B:VAL212 4.7 36.3 1.0 CB B:ILE250 4.8 37.3 1.0

D.C.Mckinney, C.J.Eyermann, R.F.Gu, J.Hu, S.L.Kazmirski, S.D.Lahiri, A.R.Mckenzie, A.B.Shapiro, G.Breault. Antibacterial Fabh Inhibitors with Mode of Action Validated in Haemophilus Influenzae By in Vitro Resistance Mutation Mapping. Acs Infect Dis. V. 2 456 2016.
ISSN: ESSN 2373-8227
PubMed: 27626097
DOI: 10.1021/ACSINFECDIS.6B00053