Fluorine in PDB 8pgi: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2984

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2984, PDB code: 8pgi 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)	40.12 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.318, 67.975, 40.204, 90, 93.78, 90
R / Rfree (%)	15.4 / 19.3

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2984 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 2984 (pdb code 8pgi). 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 2984, PDB code: 8pgi:
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 2984


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 2984 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:22.1 occ:0.60 F21 A:YRX303 0.0 22.1 0.6 H131 A:YRX303 0.4 21.5 0.4 C20 A:YRX303 1.4 21.4 0.6 C13 A:YRX303 1.4 17.9 0.4 C22 A:YRX303 2.4 19.8 0.6 C14 A:YRX303 2.4 22.0 0.6 C12 A:YRX303 2.4 17.2 0.4 C14 A:YRX303 2.4 18.9 0.4 H152 A:YRX303 2.6 28.3 0.6 H152 A:YRX303 2.6 23.9 0.4 H221 A:YRX303 2.6 23.7 0.6 H121 A:YRX303 2.6 20.6 0.4 HB2 A:HIS240 2.7 21.3 1.0 O A:HOH461 2.7 23.2 0.9 H171 A:YRX303 2.7 29.0 0.6 H171 A:YRX303 2.7 25.2 0.4 C15 A:YRX303 2.9 23.6 0.6 C15 A:YRX303 2.9 19.9 0.4 H172 A:YRX303 3.0 29.0 0.6 O A:HOH646 3.0 22.4 0.8 H173 A:YRX303 3.1 25.2 0.4 C17 A:YRX303 3.2 24.2 0.6 C17 A:YRX303 3.3 21.0 0.4 O A:HOH491 3.3 16.2 0.9 HB3 A:HIS240 3.4 21.3 1.0 CB A:HIS240 3.4 17.8 1.0 C11 A:YRX303 3.7 19.2 0.6 C13 A:YRX303 3.7 21.0 0.6 C11 A:YRX303 3.7 17.2 0.4 C20 A:YRX303 3.7 18.9 0.4 S16 A:YRX303 3.7 24.8 0.6 S16 A:YRX303 3.8 21.1 0.4 H151 A:YRX303 3.9 28.3 0.6 H151 A:YRX303 3.9 23.9 0.4 HE1 A:HIS201 3.9 27.3 1.0 CG A:HIS240 3.9 18.0 1.0 C12 A:YRX303 4.2 20.1 0.6 ND1 A:HIS201 4.2 21.5 1.0 C22 A:YRX303 4.2 17.9 0.4 H173 A:YRX303 4.2 29.0 0.6 H172 A:YRX303 4.3 25.2 0.4 HD2 A:HIS240 4.3 20.3 1.0 CD2 A:HIS240 4.4 16.9 1.0 CE1 A:HIS201 4.4 22.7 1.0 O A:HOH695 4.4 32.1 0.8 O A:HIS240 4.4 17.3 1.0 HA2 A:GLY209 4.5 28.0 1.0 H131 A:YRX303 4.6 25.2 0.6 HA3 A:GLY209 4.6 28.0 1.0 O09 A:YRX303 4.6 18.1 0.6 CA A:HIS240 4.7 17.2 1.0 O18 A:YRX303 4.7 24.4 0.6 C A:HIS240 4.7 16.3 1.0 O A:HOH493 4.7 14.7 0.8 O19 A:YRX303 4.7 19.4 0.4 ND1 A:HIS240 4.8 17.4 1.0 F21 A:YRX303 4.8 20.0 0.4 O19 A:YRX303 4.9 25.0 0.6 C10 A:YRX303 4.9 17.8 0.6 O18 A:YRX303 4.9 21.8 0.4 C10 A:YRX303 4.9 16.3 0.4 HG2 A:GLU202 5.0 20.9 1.0 O09 A:YRX303 5.0 17.7 0.4 HD1 A:HIS240 5.0 20.9 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2984


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 2984 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:20.0 occ:0.40 F21 A:YRX303 0.0 20.0 0.4 H131 A:YRX303 0.3 25.2 0.6 C13 A:YRX303 1.4 21.0 0.6 C20 A:YRX303 1.4 18.9 0.4 C12 A:YRX303 2.3 20.1 0.6 C22 A:YRX303 2.4 17.9 0.4 C14 A:YRX303 2.4 18.9 0.4 C14 A:YRX303 2.4 22.0 0.6 H151 A:YRX303 2.4 23.9 0.4 H121 A:YRX303 2.5 24.1 0.6 H151 A:YRX303 2.6 28.3 0.6 H221 A:YRX303 2.6 21.5 0.4 C15 A:YRX303 2.8 19.9 0.4 C15 A:YRX303 2.9 23.6 0.6 HE1 A:TYR67 3.0 21.2 1.0 O A:HOH526 3.2 50.8 1.0 HA2 A:GLY209 3.3 28.0 1.0 O19 A:YRX303 3.3 25.0 0.6 O19 A:YRX303 3.4 19.4 0.4 C11 A:YRX303 3.6 19.2 0.6 C11 A:YRX303 3.6 17.2 0.4 C13 A:YRX303 3.6 17.9 0.4 C20 A:YRX303 3.7 21.4 0.6 S16 A:YRX303 3.7 24.8 0.6 S16 A:YRX303 3.7 21.1 0.4 CE1 A:TYR67 3.7 17.7 1.0 H152 A:YRX303 3.8 23.9 0.4 H152 A:YRX303 3.9 28.3 0.6 C22 A:YRX303 4.1 19.8 0.6 C12 A:YRX303 4.1 17.2 0.4 CA A:GLY209 4.2 23.4 1.0 HD1 A:TYR67 4.2 20.4 1.0 H241 A:YRX303 4.4 18.9 0.4 CD1 A:TYR67 4.4 17.0 1.0 O A:HOH467 4.4 30.8 0.6 H172 A:YRX303 4.5 29.0 0.6 H241 A:YRX303 4.5 21.9 0.6 H131 A:YRX303 4.5 21.5 0.4 C A:GLY209 4.6 22.2 1.0 CZ A:TYR67 4.6 17.8 1.0 HA3 A:GLY209 4.6 28.0 1.0 OH A:TYR67 4.6 19.1 1.0 O18 A:YRX303 4.7 21.8 0.4 H A:GLY209 4.8 30.1 1.0 C17 A:YRX303 4.8 24.2 0.6 F21 A:YRX303 4.8 22.1 0.6 O18 A:YRX303 4.8 24.4 0.6 O A:HOH695 4.8 32.1 0.8 C10 A:YRX303 4.9 17.8 0.6 H171 A:YRX303 4.9 25.2 0.4 C10 A:YRX303 4.9 16.3 0.4 O A:GLY209 5.0 22.9 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 2984 To Be Published.