Fluorine in PDB 8pb0: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2696

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2696, PDB code: 8pb0 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)	28.99 / 1.26
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.49, 67.91, 40.22, 90, 93.37, 90
R / Rfree (%)	13.5 / 16

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2696 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 2696 (pdb code 8pb0). 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 2696, PDB code: 8pb0:
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 2696


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 2696 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:13.7 occ:0.24 F21 A:XQE303 0.0 13.7 0.2 H131 A:XQE303 0.3 21.7 0.8 C13 A:XQE303 1.3 18.1 0.8 C20 A:XQE303 1.4 15.7 0.2 C12 A:XQE303 2.3 16.5 0.8 C22 A:XQE303 2.4 16.0 0.2 C14 A:XQE303 2.4 18.7 0.8 C14 A:XQE303 2.4 17.2 0.2 H152 A:XQE303 2.5 22.7 0.2 H152 A:XQE303 2.5 23.7 0.8 H121 A:XQE303 2.5 19.8 0.8 H221 A:XQE303 2.6 19.2 0.2 HE2 A:TYR67 2.7 18.3 1.0 C15 A:XQE303 2.8 18.9 0.2 C15 A:XQE303 2.9 19.8 0.8 O18 A:XQE303 3.2 20.0 0.2 HA2 A:GLY209 3.3 24.1 1.0 O18 A:XQE303 3.3 22.7 0.8 CE2 A:TYR67 3.5 15.2 1.0 C11 A:XQE303 3.6 15.3 0.8 C20 A:XQE303 3.6 18.6 0.8 C11 A:XQE303 3.6 16.3 0.2 C13 A:XQE303 3.6 16.9 0.2 S16 A:XQE303 3.6 20.8 0.2 H151 A:XQE303 3.8 22.7 0.2 S16 A:XQE303 3.8 21.8 0.8 H151 A:XQE303 3.8 23.7 0.8 HD2 A:TYR67 4.0 18.6 1.0 C22 A:XQE303 4.1 16.7 0.8 C12 A:XQE303 4.1 16.5 0.2 CD2 A:TYR67 4.2 15.5 1.0 CA A:GLY209 4.2 20.1 1.0 H241 A:XQE303 4.3 14.5 0.8 O A:HOH640 4.3 26.9 0.8 H241 A:XQE303 4.3 19.8 0.2 CZ A:TYR67 4.5 14.5 1.0 OH A:TYR67 4.5 15.8 1.0 H131 A:XQE303 4.5 20.3 0.2 O19 A:XQE303 4.5 21.9 0.2 O A:HOH711 4.6 28.2 0.8 HA3 A:GLY209 4.7 24.1 1.0 O A:HOH512 4.7 31.4 0.7 C A:GLY209 4.7 20.8 1.0 F21 A:XQE303 4.7 20.7 0.8 H A:GLY209 4.8 26.1 1.0 H173 A:XQE303 4.8 26.9 0.8 H173 A:XQE303 4.8 25.4 0.2 C10 A:XQE303 4.8 12.3 0.8 O19 A:XQE303 4.9 21.4 0.8 C10 A:XQE303 4.9 16.3 0.2 C17 A:XQE303 5.0 21.1 0.2

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2696


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 2696 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:20.7 occ:0.76 F21 A:XQE303 0.0 20.7 0.8 H131 A:XQE303 0.3 20.3 0.2 C13 A:XQE303 1.3 16.9 0.2 C20 A:XQE303 1.4 18.6 0.8 C12 A:XQE303 2.3 16.5 0.2 C22 A:XQE303 2.4 16.7 0.8 H173 A:XQE303 2.4 25.4 0.2 C14 A:XQE303 2.4 17.2 0.2 C14 A:XQE303 2.4 18.7 0.8 H173 A:XQE303 2.5 26.9 0.8 H121 A:XQE303 2.5 19.8 0.2 H151 A:XQE303 2.5 23.7 0.8 H151 A:XQE303 2.6 22.7 0.2 H221 A:XQE303 2.6 20.0 0.8 HB2 A:HIS240 2.6 14.3 1.0 C15 A:XQE303 2.9 19.8 0.8 O A:HOH464 2.9 15.9 0.8 C15 A:XQE303 2.9 18.9 0.2 C17 A:XQE303 3.2 22.4 0.8 H172 A:XQE303 3.2 26.9 0.8 C17 A:XQE303 3.2 21.1 0.2 O A:HOH658 3.2 21.3 0.9 HB3 A:HIS240 3.3 14.3 1.0 CB A:HIS240 3.3 11.9 1.0 O A:HOH500 3.4 12.0 0.8 H172 A:XQE303 3.4 25.4 0.2 HD1 A:HIS201 3.5 23.1 0.5 C11 A:XQE303 3.6 16.3 0.2 C20 A:XQE303 3.6 15.7 0.2 HE1 A:HIS201 3.6 25.3 1.0 C13 A:XQE303 3.6 18.1 0.8 C11 A:XQE303 3.6 15.3 0.8 S16 A:XQE303 3.7 21.8 0.8 S16 A:XQE303 3.8 20.8 0.2 H152 A:XQE303 3.8 23.7 0.8 CG A:HIS240 3.8 11.8 1.0 H152 A:XQE303 3.9 22.7 0.2 ND1 A:HIS201 4.1 19.2 1.0 C22 A:XQE303 4.1 16.0 0.2 H171 A:XQE303 4.1 25.4 0.2 C12 A:XQE303 4.1 16.5 0.8 H171 A:XQE303 4.1 26.9 0.8 CE1 A:HIS201 4.2 21.1 1.0 HD2 A:HIS240 4.2 14.4 1.0 CD2 A:HIS240 4.2 12.0 1.0 O08 A:XQE303 4.4 18.0 0.2 HA2 A:GLY209 4.4 24.1 1.0 HA3 A:GLY209 4.4 24.1 1.0 O A:HOH711 4.5 28.2 0.8 O A:HIS240 4.5 12.3 1.0 H131 A:XQE303 4.5 21.7 0.8 O18 A:XQE303 4.6 20.0 0.2 CA A:HIS240 4.6 11.2 1.0 ND1 A:HIS240 4.6 12.0 1.0 O18 A:XQE303 4.6 22.7 0.8 O A:HOH481 4.6 9.6 0.7 O19 A:XQE303 4.7 21.4 0.8 O08 A:XQE303 4.7 13.5 0.8 F21 A:XQE303 4.7 13.7 0.2 C A:HIS240 4.8 11.3 1.0 C10 A:XQE303 4.8 16.3 0.2 C07 A:XQE303 4.8 17.2 0.2 C10 A:XQE303 4.8 12.3 0.8 CA A:GLY209 4.9 20.1 1.0 HD1 A:HIS240 4.9 14.4 1.0 O19 A:XQE303 5.0 21.9 0.2 O A:HOH457 5.0 11.9 0.7 C07 A:XQE303 5.0 11.9 0.8 HD2 A:TYR67 5.0 18.6 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 2696 To Be Published.