Fluorine in PDB 8pgo: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183, PDB code: 8pgo was solved by K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.44 / 1.14
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.41, 67.67, 40.08, 90, 93.39, 90
R / Rfree (%)	12.5 / 13.5

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Fluorine atom in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183 (pdb code 8pgo). 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 the Metallo-Beta-Lactamase VIM1 with 3183, PDB code: 8pgo:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183


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 the Metallo-Beta-Lactamase VIM1 with 3183 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:21.6 occ:0.75 F21 A:YUQ303 0.0 21.6 0.8 F21 A:YUQ303 1.3 15.9 0.2 C20 A:YUQ303 1.4 20.5 0.8 C20 A:YUQ303 2.1 16.2 0.2 H221 A:YUQ303 2.3 18.7 0.2 C22 A:YUQ303 2.4 18.0 0.8 HB2 A:HIS240 2.4 14.1 1.0 C14 A:YUQ303 2.4 20.8 0.8 C22 A:YUQ303 2.5 15.6 0.2 H171 A:YUQ303 2.5 29.2 0.8 H221 A:YUQ303 2.6 21.6 0.8 N15 A:YUQ303 2.8 22.6 0.8 O A:HOH436 3.0 15.4 0.6 HD1 A:HIS201 3.1 21.3 1.0 O A:HOH526 3.1 13.3 1.0 HE1 A:HIS201 3.1 22.1 1.0 H151 A:YUQ303 3.1 27.1 0.8 CB A:HIS240 3.2 11.8 1.0 C14 A:YUQ303 3.3 17.3 0.2 HB3 A:HIS240 3.4 14.1 1.0 C17 A:YUQ303 3.4 24.3 0.8 H151 A:YUQ303 3.4 23.5 0.2 O A:HOH669 3.6 18.5 0.6 ND1 A:HIS201 3.6 17.7 1.0 C11 A:YUQ303 3.6 15.7 0.8 CE1 A:HIS201 3.7 18.4 1.0 C13 A:YUQ303 3.7 19.4 0.8 CG A:HIS240 3.7 11.3 1.0 H172 A:YUQ303 3.7 29.2 0.8 S16 A:YUQ303 3.8 24.7 0.8 N15 A:YUQ303 3.8 19.6 0.2 C11 A:YUQ303 3.8 15.6 0.2 HD2 A:HIS240 3.9 14.1 1.0 CD2 A:HIS240 4.0 11.7 1.0 O09 A:YUQ303 4.0 15.4 0.2 O A:HOH510 4.1 10.1 0.8 C12 A:YUQ303 4.2 17.6 0.8 HA3 A:GLY209 4.2 22.4 1.0 H173 A:YUQ303 4.2 29.2 0.8 O A:HIS240 4.3 11.8 1.0 HA2 A:GLY209 4.3 22.4 1.0 O09 A:YUQ303 4.3 12.8 0.8 C13 A:YUQ303 4.4 16.1 0.2 CA A:HIS240 4.5 11.4 1.0 O A:HOH470 4.5 10.6 0.6 H131 A:YUQ303 4.6 23.3 0.8 C07 A:YUQ303 4.6 15.2 0.2 C12 A:YUQ303 4.6 15.8 0.2 C A:HIS240 4.6 11.3 1.0 ND1 A:HIS240 4.6 11.9 1.0 C07 A:YUQ303 4.7 12.1 0.8 H A:HIS240 4.7 12.3 1.0 O19 A:YUQ303 4.7 25.0 0.8 CA A:GLY209 4.8 18.7 1.0 C10 A:YUQ303 4.8 12.8 0.8 O A:HOH640 4.8 32.3 0.8 C10 A:YUQ303 4.8 15.5 0.2 O18 A:YUQ303 4.8 25.1 0.8 N A:HIS240 5.0 10.2 1.0 HD1 A:HIS240 5.0 14.2 0.7 CG A:HIS201 5.0 16.5 1.0 NE2 A:HIS201 5.0 18.9 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183


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 the Metallo-Beta-Lactamase VIM1 with 3183 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:15.9 occ:0.25 F21 A:YUQ303 0.0 15.9 0.2 C20 A:YUQ303 1.3 20.5 0.8 F21 A:YUQ303 1.3 21.6 0.8 C20 A:YUQ303 1.4 16.2 0.2 C14 A:YUQ303 1.5 20.8 0.8 N15 A:YUQ303 1.8 22.6 0.8 H151 A:YUQ303 2.0 27.1 0.8 C14 A:YUQ303 2.4 17.3 0.2 H151 A:YUQ303 2.4 23.5 0.2 C22 A:YUQ303 2.4 15.6 0.2 C22 A:YUQ303 2.5 18.0 0.8 H221 A:YUQ303 2.6 18.7 0.2 N15 A:YUQ303 2.7 19.6 0.2 O A:HOH436 2.7 15.4 0.6 H171 A:YUQ303 2.8 29.2 0.8 C13 A:YUQ303 2.9 19.4 0.8 O A:HOH669 3.0 18.5 0.6 H221 A:YUQ303 3.2 21.6 0.8 S16 A:YUQ303 3.2 24.7 0.8 HB2 A:HIS240 3.2 14.1 1.0 C17 A:YUQ303 3.4 24.3 0.8 C11 A:YUQ303 3.5 15.7 0.8 H131 A:YUQ303 3.6 23.3 0.8 C11 A:YUQ303 3.6 15.6 0.2 C13 A:YUQ303 3.6 16.1 0.2 C12 A:YUQ303 3.6 17.6 0.8 O A:HOH640 3.7 32.3 0.8 HB3 A:HIS240 3.7 14.1 1.0 H172 A:YUQ303 3.9 29.2 0.8 CB A:HIS240 3.9 11.8 1.0 O A:HOH526 3.9 13.3 1.0 HD1 A:HIS201 4.0 21.3 1.0 HE1 A:HIS201 4.1 22.1 1.0 O19 A:YUQ303 4.1 25.0 0.8 C12 A:YUQ303 4.1 15.8 0.2 O18 A:YUQ303 4.2 25.1 0.8 HA2 A:GLY209 4.2 22.4 1.0 S16 A:YUQ303 4.3 22.1 0.2 H173 A:YUQ303 4.4 29.2 0.8 CG A:HIS240 4.4 11.3 1.0 H131 A:YUQ303 4.5 19.4 0.2 HA3 A:GLY209 4.6 22.4 1.0 ND1 A:HIS201 4.6 17.7 1.0 HD1 A:TYR67 4.6 16.1 1.0 CE1 A:HIS201 4.7 18.4 1.0 H121 A:YUQ303 4.7 21.2 0.8 O09 A:YUQ303 4.7 15.4 0.2 O18 A:YUQ303 4.8 22.4 0.2 O19 A:YUQ303 4.8 22.6 0.2 CA A:GLY209 4.8 18.7 1.0 C10 A:YUQ303 4.9 12.8 0.8 CD2 A:HIS240 4.9 11.7 1.0 C10 A:YUQ303 4.9 15.5 0.2 HD2 A:HIS240 5.0 14.1 1.0

K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield. Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3183 To Be Published.