Fluorine in PDB 8pb2: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2697

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2697, PDB code: 8pb2 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)	29.04 / 1.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.5, 67.929, 40.256, 90, 93.51, 90
R / Rfree (%)	10.8 / 12.5

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2697 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 2697 (pdb code 8pb2). 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 2697, PDB code: 8pb2:
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 2697


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 2697 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:17.5 occ:0.45 F21 A:XQ5303 0.0 17.5 0.5 H131 A:XQ5303 0.3 19.6 0.6 C13 A:XQ5303 1.4 16.3 0.6 C20 A:XQ5303 1.4 16.6 0.5 C12 A:XQ5303 2.4 15.1 0.6 C22 A:XQ5303 2.4 15.3 0.5 C14 A:XQ5303 2.4 16.5 0.5 C14 A:XQ5303 2.4 16.9 0.6 H151 A:XQ5303 2.5 21.0 0.5 H151 A:XQ5303 2.5 23.2 0.6 H121 A:XQ5303 2.6 18.1 0.6 H221 A:XQ5303 2.6 18.3 0.5 C15 A:XQ5303 2.9 17.5 0.5 C15 A:XQ5303 2.9 19.4 0.6 HE2 A:TYR67 2.9 15.8 1.0 O19 A:XQ5303 3.2 23.1 0.6 O A:HOH610 3.2 48.5 1.0 O19 A:XQ5303 3.3 16.9 0.5 HA2 A:GLY209 3.3 23.4 1.0 C11 A:XQ5303 3.6 13.9 0.6 C13 A:XQ5303 3.6 16.5 0.5 C11 A:XQ5303 3.6 14.3 0.5 C20 A:XQ5303 3.6 16.7 0.6 S16 A:XQ5303 3.7 22.1 0.6 CE2 A:TYR67 3.7 13.2 1.0 S16 A:XQ5303 3.7 18.2 0.5 H152 A:XQ5303 3.8 21.0 0.5 H152 A:XQ5303 3.8 23.2 0.6 C12 A:XQ5303 4.1 15.1 0.5 C22 A:XQ5303 4.1 14.9 0.6 HD2 A:TYR67 4.1 15.8 1.0 CA A:GLY209 4.3 19.5 1.0 CD2 A:TYR67 4.3 13.2 1.0 H241 A:XQ5303 4.4 14.8 0.5 O A:HOH761 4.4 30.0 0.8 H241 A:XQ5303 4.4 14.9 0.6 O A:HOH661 4.4 32.2 1.0 H131 A:XQ5303 4.5 19.8 0.5 CZ A:TYR67 4.6 12.6 1.0 H171 A:XQ5303 4.6 25.9 0.6 OH A:TYR67 4.6 14.5 1.0 C A:GLY209 4.7 19.3 1.0 HA3 A:GLY209 4.7 23.4 1.0 O18 A:XQ5303 4.7 21.6 0.6 H171 A:XQ5303 4.7 22.8 0.5 O18 A:XQ5303 4.8 19.8 0.5 F21 A:XQ5303 4.8 17.1 0.6 H A:GLY209 4.8 25.9 1.0 O A:HOH491 4.9 33.1 0.8 C17 A:XQ5303 4.9 21.6 0.6 HG A:SER207 4.9 43.6 1.0 C10 A:XQ5303 4.9 12.4 0.5 C10 A:XQ5303 4.9 11.4 0.6 C17 A:XQ5303 5.0 19.1 0.5

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2697


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 2697 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:17.1 occ:0.55 F21 A:XQ5303 0.0 17.1 0.6 H131 A:XQ5303 0.4 19.8 0.5 C13 A:XQ5303 1.3 16.5 0.5 C20 A:XQ5303 1.4 16.7 0.6 C12 A:XQ5303 2.3 15.1 0.5 C22 A:XQ5303 2.4 14.9 0.6 C14 A:XQ5303 2.4 16.9 0.6 C14 A:XQ5303 2.4 16.5 0.5 H152 A:XQ5303 2.4 23.2 0.6 H121 A:XQ5303 2.5 18.1 0.5 H152 A:XQ5303 2.6 21.0 0.5 H221 A:XQ5303 2.6 17.9 0.6 HB2 A:HIS240 2.6 12.8 1.0 H171 A:XQ5303 2.7 22.8 0.5 O A:HOH463 2.8 14.2 0.7 C15 A:XQ5303 2.8 19.4 0.6 H173 A:XQ5303 2.9 25.9 0.6 H171 A:XQ5303 2.9 25.9 0.6 C15 A:XQ5303 2.9 17.5 0.5 H173 A:XQ5303 3.0 22.8 0.5 O A:HOH678 3.2 17.9 0.8 C17 A:XQ5303 3.2 19.1 0.5 HB3 A:HIS240 3.2 12.8 1.0 C17 A:XQ5303 3.3 21.6 0.6 CB A:HIS240 3.3 10.7 1.0 O A:HOH532 3.3 11.7 0.9 HD1 A:HIS201 3.5 20.6 0.4 C11 A:XQ5303 3.6 14.3 0.5 C20 A:XQ5303 3.6 16.6 0.5 C11 A:XQ5303 3.6 13.9 0.6 HE1 A:HIS201 3.6 22.6 1.0 C13 A:XQ5303 3.6 16.3 0.6 S16 A:XQ5303 3.7 22.1 0.6 H151 A:XQ5303 3.8 23.2 0.6 S16 A:XQ5303 3.8 18.2 0.5 CG A:HIS240 3.8 10.5 1.0 H151 A:XQ5303 3.9 21.0 0.5 ND1 A:HIS201 4.1 17.2 1.0 C22 A:XQ5303 4.1 15.3 0.5 C12 A:XQ5303 4.1 15.1 0.6 CE1 A:HIS201 4.2 18.8 1.0 H172 A:XQ5303 4.2 22.8 0.5 HD2 A:HIS240 4.3 12.7 1.0 CD2 A:HIS240 4.3 10.6 1.0 H172 A:XQ5303 4.3 25.9 0.6 O A:HOH761 4.4 30.0 0.8 O A:HIS240 4.5 10.8 1.0 HA2 A:GLY209 4.5 23.4 1.0 H131 A:XQ5303 4.5 19.6 0.6 HA3 A:GLY209 4.5 23.4 1.0 CA A:HIS240 4.6 9.5 1.0 ND1 A:HIS240 4.6 11.4 1.0 O A:HOH493 4.6 9.4 0.8 O09 A:XQ5303 4.6 15.9 0.5 O19 A:XQ5303 4.7 16.9 0.5 C A:HIS240 4.7 10.0 1.0 O18 A:XQ5303 4.7 21.6 0.6 O09 A:XQ5303 4.7 11.9 0.6 O19 A:XQ5303 4.7 23.1 0.6 F21 A:XQ5303 4.8 17.5 0.5 C10 A:XQ5303 4.8 12.4 0.5 HD1 A:HIS240 4.8 13.7 1.0 C10 A:XQ5303 4.9 11.4 0.6 O18 A:XQ5303 4.9 19.8 0.5 CA A:GLY209 5.0 19.5 1.0 C07 A:XQ5303 5.0 13.9 0.5

K.Calvopina, J.Brem, A.J.M.Farley, M.D.Allen, C.J.Schofield. Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2697 To Be Published.