Fluorine in PDB 8pgl: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3027

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3027, PDB code: 8pgl 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)	34.63 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.51, 68.06, 40.31, 90, 93.83, 90
R / Rfree (%)	13 / 14.3

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3027 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 3027 (pdb code 8pgl). 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 3027, PDB code: 8pgl:
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 3027


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 3027 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:21.7 occ:0.68 F21 A:YK5303 0.0 21.7 0.7 H131 A:YK5303 0.3 20.1 0.3 C13 A:YK5303 1.3 16.8 0.3 C20 A:YK5303 1.3 18.8 0.7 H171 A:YK5303 2.3 27.9 0.3 C12 A:YK5303 2.3 15.6 0.3 C22 A:YK5303 2.3 16.2 0.7 C14 A:YK5303 2.4 18.5 0.7 C14 A:YK5303 2.4 18.1 0.3 H121 A:YK5303 2.5 18.7 0.3 H151 A:YK5303 2.5 24.6 0.7 H171 A:YK5303 2.5 25.6 0.7 H221 A:YK5303 2.6 19.5 0.7 H151 A:YK5303 2.6 25.5 0.3 HB2 A:HIS240 2.7 16.0 1.0 O A:HOH452 2.7 14.2 0.6 C15 A:YK5303 2.9 20.5 0.7 C15 A:YK5303 2.9 21.3 0.3 C17 A:YK5303 3.0 23.3 0.3 H172 A:YK5303 3.1 27.9 0.3 C17 A:YK5303 3.2 21.4 0.7 H172 A:YK5303 3.2 25.6 0.7 O A:HOH509 3.2 12.3 0.8 O A:HOH630 3.3 16.2 0.5 HB3 A:HIS240 3.4 16.0 1.0 CB A:HIS240 3.4 13.3 1.0 HE1 A:HIS201 3.5 26.5 1.0 C11 A:YK5303 3.6 15.6 0.3 C11 A:YK5303 3.6 15.7 0.7 C20 A:YK5303 3.6 16.6 0.3 C13 A:YK5303 3.6 17.7 0.7 S16 A:YK5303 3.7 23.0 0.3 S16 A:YK5303 3.8 21.1 0.7 H152 A:YK5303 3.8 24.6 0.7 H152 A:YK5303 3.9 25.5 0.3 ND1 A:HIS201 3.9 19.7 1.0 CG A:HIS240 3.9 13.2 1.0 H173 A:YK5303 4.0 27.9 0.3 CE1 A:HIS201 4.0 22.1 1.0 C22 A:YK5303 4.1 16.0 0.3 C12 A:YK5303 4.1 16.6 0.7 H173 A:YK5303 4.2 25.6 0.7 HD2 A:HIS240 4.3 15.2 1.0 CD2 A:HIS240 4.3 12.7 1.0 HA3 A:GLY209 4.4 25.5 1.0 HA2 A:GLY209 4.4 25.5 1.0 O09 A:YK5303 4.4 16.3 0.3 O A:HIS240 4.5 13.2 1.0 O A:HOH682 4.5 31.5 0.8 H131 A:YK5303 4.5 21.2 0.7 O A:HOH473 4.6 11.8 0.8 O18 A:YK5303 4.6 22.7 0.3 O19 A:YK5303 4.6 20.4 0.7 O09 A:YK5303 4.7 13.8 0.7 CA A:HIS240 4.7 12.2 1.0 O19 A:YK5303 4.7 23.5 0.3 F21 A:YK5303 4.7 15.1 0.3 C A:HIS240 4.8 12.4 1.0 ND1 A:HIS240 4.8 13.2 1.0 C10 A:YK5303 4.8 14.7 0.3 O18 A:YK5303 4.8 22.9 0.7 C10 A:YK5303 4.8 13.1 0.7 C07 A:YK5303 4.9 15.5 0.3 CA A:GLY209 4.9 21.2 1.0 HG2 A:GLU202 5.0 18.4 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3027


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 3027 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:15.1 occ:0.32 F21 A:YK5303 0.0 15.1 0.3 H131 A:YK5303 0.3 21.2 0.7 C13 A:YK5303 1.3 17.7 0.7 C20 A:YK5303 1.3 16.6 0.3 C12 A:YK5303 2.3 16.6 0.7 C14 A:YK5303 2.4 18.1 0.3 C14 A:YK5303 2.4 18.5 0.7 C22 A:YK5303 2.4 16.0 0.3 H152 A:YK5303 2.5 25.5 0.3 H152 A:YK5303 2.5 24.6 0.7 H121 A:YK5303 2.6 19.9 0.7 H221 A:YK5303 2.6 19.2 0.3 C15 A:YK5303 2.8 21.3 0.3 C15 A:YK5303 2.9 20.5 0.7 HE1 A:TYR67 2.9 19.4 1.0 O19 A:YK5303 3.2 20.4 0.7 O19 A:YK5303 3.3 23.5 0.3 HA2 A:GLY209 3.4 25.5 1.0 O A:DMS304 3.4 31.3 0.7 O A:HOH597 3.4 39.1 0.8 C11 A:YK5303 3.6 15.7 0.7 C20 A:YK5303 3.6 18.8 0.7 C13 A:YK5303 3.6 16.8 0.3 C11 A:YK5303 3.6 15.6 0.3 CE1 A:TYR67 3.7 16.2 1.0 S16 A:YK5303 3.7 21.1 0.7 S16 A:YK5303 3.7 23.0 0.3 H151 A:YK5303 3.8 25.5 0.3 H151 A:YK5303 3.8 24.6 0.7 C22 A:YK5303 4.1 16.2 0.7 HD1 A:TYR67 4.1 18.5 1.0 C12 A:YK5303 4.1 15.6 0.3 CA A:GLY209 4.3 21.2 1.0 CD1 A:TYR67 4.3 15.4 1.0 H241 A:YK5303 4.3 16.2 0.7 O A:HOH682 4.4 31.5 0.8 S A:DMS304 4.5 30.3 0.7 H241 A:YK5303 4.5 18.7 0.3 H131 A:YK5303 4.5 20.1 0.3 O A:HOH471 4.5 29.3 0.6 H172 A:YK5303 4.6 27.9 0.3 CZ A:TYR67 4.6 15.6 1.0 OH A:TYR67 4.6 16.9 1.0 HA3 A:GLY209 4.7 25.5 1.0 C A:GLY209 4.7 20.9 1.0 F21 A:YK5303 4.7 21.7 0.7 O18 A:YK5303 4.7 22.9 0.7 C17 A:YK5303 4.8 23.3 0.3 O18 A:YK5303 4.8 22.7 0.3 H172 A:YK5303 4.9 25.6 0.7 C10 A:YK5303 4.9 13.1 0.7 C10 A:YK5303 4.9 14.7 0.3 H A:GLY209 5.0 27.4 1.0 C17 A:YK5303 5.0 21.4 0.7

K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield. Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 3027 To Be Published.