Fluorine in PDB 8pgj: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2985

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2985, PDB code: 8pgj 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)	34.05 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.404, 68.127, 40.283, 90, 93.77, 90
R / Rfree (%)	12 / 13.7

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2985 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 2985 (pdb code 8pgj). 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 2985, PDB code: 8pgj:
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 2985


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 2985 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:15.6 occ:0.55 F21 A:YMB303 0.0 15.6 0.6 H131 A:YMB303 0.4 16.4 0.5 C20 A:YMB303 1.4 14.5 0.6 C13 A:YMB303 1.4 13.7 0.5 C14 A:YMB303 2.3 14.4 0.6 C22 A:YMB303 2.4 13.3 0.6 C14 A:YMB303 2.4 13.8 0.5 C12 A:YMB303 2.4 13.5 0.5 H151 A:YMB303 2.4 19.8 0.6 H151 A:YMB303 2.6 17.5 0.5 H221 A:YMB303 2.6 16.0 0.6 H121 A:YMB303 2.6 16.2 0.5 C15 A:YMB303 2.8 16.5 0.6 HE1 A:TYR67 2.9 15.7 1.0 C15 A:YMB303 2.9 14.6 0.5 O18 A:YMB303 3.2 18.5 0.6 O18 A:YMB303 3.3 16.2 0.5 O A:DMS304 3.4 28.0 0.6 HA2 A:GLY209 3.4 21.6 1.0 C13 A:YMB303 3.6 13.7 0.6 C11 A:YMB303 3.6 11.7 0.6 C20 A:YMB303 3.6 13.9 0.5 C11 A:YMB303 3.7 12.7 0.5 S16 A:YMB303 3.7 18.0 0.6 CE1 A:TYR67 3.7 13.1 1.0 H152 A:YMB303 3.8 19.8 0.6 S16 A:YMB303 3.8 15.4 0.5 H152 A:YMB303 3.9 17.5 0.5 C12 A:YMB303 4.1 12.3 0.6 HD1 A:TYR67 4.1 15.2 1.0 C22 A:YMB303 4.1 13.1 0.5 CD1 A:TYR67 4.3 12.7 1.0 H241 A:YMB303 4.3 14.0 0.5 CA A:GLY209 4.3 18.0 1.0 H241 A:YMB303 4.4 13.7 0.6 S A:DMS304 4.4 27.7 0.6 H131 A:YMB303 4.5 16.4 0.6 O A:HOH702 4.5 28.6 0.8 H173 A:YMB303 4.6 22.7 0.6 CZ A:TYR67 4.6 12.8 1.0 O A:HOH489 4.6 29.8 0.7 OH A:TYR67 4.6 14.0 1.0 O19 A:YMB303 4.7 17.3 0.6 H172 A:YMB303 4.7 18.6 0.5 F21 A:YMB303 4.7 14.5 0.5 HA3 A:GLY209 4.7 21.6 1.0 C A:GLY209 4.8 17.1 1.0 O19 A:YMB303 4.8 17.0 0.5 C10 A:YMB303 4.8 9.7 0.6 C17 A:YMB303 4.9 18.9 0.6 C10 A:YMB303 4.9 11.8 0.5 C17 A:YMB303 5.0 15.5 0.5 H A:GLY209 5.0 23.3 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2985


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 2985 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:14.5 occ:0.45 F21 A:YMB303 0.0 14.5 0.5 H131 A:YMB303 0.3 16.4 0.6 C13 A:YMB303 1.3 13.7 0.6 C20 A:YMB303 1.4 13.9 0.5 C12 A:YMB303 2.3 12.3 0.6 C22 A:YMB303 2.3 13.1 0.5 C14 A:YMB303 2.4 13.8 0.5 C14 A:YMB303 2.4 14.4 0.6 H152 A:YMB303 2.4 17.5 0.5 H121 A:YMB303 2.5 14.8 0.6 H221 A:YMB303 2.5 15.8 0.5 H152 A:YMB303 2.6 19.8 0.6 HB2 A:HIS240 2.7 12.6 1.0 H173 A:YMB303 2.7 22.7 0.6 H172 A:YMB303 2.7 18.6 0.5 O A:HOH465 2.7 14.1 0.7 H172 A:YMB303 2.8 22.7 0.6 C15 A:YMB303 2.8 14.6 0.5 C15 A:YMB303 2.9 16.5 0.6 H171 A:YMB303 3.0 18.6 0.5 C17 A:YMB303 3.1 18.9 0.6 C17 A:YMB303 3.2 15.5 0.5 O A:HOH534 3.2 10.5 0.8 O A:HOH640 3.3 16.1 0.7 CB A:HIS240 3.4 10.5 1.0 HB3 A:HIS240 3.4 12.6 1.0 HE1 A:HIS201 3.5 20.6 1.0 C11 A:YMB303 3.6 11.7 0.6 C11 A:YMB303 3.6 12.7 0.5 C20 A:YMB303 3.6 14.5 0.6 C13 A:YMB303 3.6 13.7 0.5 S16 A:YMB303 3.7 18.0 0.6 H151 A:YMB303 3.8 17.5 0.5 S16 A:YMB303 3.8 15.4 0.5 CG A:HIS240 3.9 10.2 1.0 ND1 A:HIS201 3.9 16.0 1.0 H151 A:YMB303 3.9 19.8 0.6 CE1 A:HIS201 4.0 17.2 1.0 C12 A:YMB303 4.1 13.5 0.5 C22 A:YMB303 4.1 13.3 0.6 H171 A:YMB303 4.1 22.7 0.6 H173 A:YMB303 4.2 18.6 0.5 HD2 A:HIS240 4.3 12.0 1.0 CD2 A:HIS240 4.3 10.0 1.0 O08 A:YMB303 4.3 13.1 0.5 HA3 A:GLY209 4.4 21.6 1.0 HA2 A:GLY209 4.4 21.6 1.0 O A:HIS240 4.5 10.3 1.0 H131 A:YMB303 4.5 16.4 0.5 O A:HOH492 4.6 9.5 0.8 O A:HOH702 4.6 28.6 0.8 O18 A:YMB303 4.6 18.5 0.6 O19 A:YMB303 4.6 17.3 0.6 O18 A:YMB303 4.7 16.2 0.5 O08 A:YMB303 4.7 8.6 0.6 CA A:HIS240 4.7 9.9 1.0 F21 A:YMB303 4.7 15.6 0.6 C10 A:YMB303 4.7 9.7 0.6 ND1 A:HIS240 4.8 10.6 1.0 C A:HIS240 4.8 9.8 1.0 C10 A:YMB303 4.8 11.8 0.5 CA A:GLY209 4.9 18.0 1.0 C07 A:YMB303 4.9 12.9 0.5 O19 A:YMB303 4.9 17.0 0.5 O A:HOH499 5.0 9.3 0.6 C07 A:YMB303 5.0 7.3 0.6

K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield. Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2985 To Be Published.