Fluorine in PDB 8pgb: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2850

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2850, PDB code: 8pgb 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)	34.66 / 1.34
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.55, 68.126, 40.335, 90, 93.62, 90
R / Rfree (%)	12.7 / 15.5

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2850 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 2850 (pdb code 8pgb). 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 2850, PDB code: 8pgb:
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 2850


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 2850 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:21.1 occ:0.50 F29 A:YSK303 0.0 21.1 0.5 H211 A:YSK303 0.4 26.0 0.5 C28 A:YSK303 1.3 20.0 0.5 C21 A:YSK303 1.4 21.7 0.5 C30 A:YSK303 2.3 19.4 0.5 C22 A:YSK303 2.4 20.0 0.5 H232 A:YSK303 2.4 31.9 0.5 C22 A:YSK303 2.4 23.4 0.5 C20 A:YSK303 2.4 20.9 0.5 H232 A:YSK303 2.5 25.2 0.5 H301 A:YSK303 2.6 23.3 0.5 H201 A:YSK303 2.6 25.1 0.5 C23 A:YSK303 2.8 26.6 0.5 C23 A:YSK303 2.9 21.0 0.5 HE1 A:TYR67 2.9 22.4 1.0 O26 A:YSK303 3.2 21.3 0.5 O26 A:YSK303 3.3 29.9 0.5 HA2 A:GLY209 3.4 28.8 1.0 O A:HOH606 3.5 44.8 0.8 C19 A:YSK303 3.6 18.1 0.5 C21 A:YSK303 3.6 19.4 0.5 C28 A:YSK303 3.7 22.1 0.5 C19 A:YSK303 3.7 19.4 0.5 S24 A:YSK303 3.7 21.4 0.5 S24 A:YSK303 3.7 29.2 0.5 CE1 A:TYR67 3.7 18.6 1.0 H231 A:YSK303 3.8 31.9 0.5 H231 A:YSK303 3.8 25.2 0.5 C20 A:YSK303 4.1 18.4 0.5 HD1 A:TYR67 4.1 21.2 1.0 C30 A:YSK303 4.1 20.5 0.5 CD1 A:TYR67 4.3 17.7 1.0 CA A:GLY209 4.3 24.0 1.0 H101 A:YSK303 4.4 19.8 0.5 H101 A:YSK303 4.4 21.2 0.5 H211 A:YSK303 4.5 23.2 0.5 O A:HOH669 4.5 24.1 0.4 O A:HOH458 4.6 33.5 0.6 CZ A:TYR67 4.6 18.4 1.0 OH A:TYR67 4.7 20.2 1.0 O27 A:YSK303 4.7 29.5 0.5 C A:GLY209 4.7 23.0 1.0 O27 A:YSK303 4.7 22.2 0.5 HA3 A:GLY209 4.8 28.8 1.0 F29 A:YSK303 4.8 22.9 0.5 H252 A:YSK303 4.8 35.2 0.5 C18 A:YSK303 4.9 16.6 0.5 C18 A:YSK303 4.9 17.3 0.5 C25 A:YSK303 4.9 29.4 0.5 H251 A:YSK303 4.9 25.3 0.5 H A:GLY209 5.0 30.5 1.0 C25 A:YSK303 5.0 21.1 0.5 HG A:SER207 5.0 43.9 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2850


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 2850 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:22.9 occ:0.50 F29 A:YSK303 0.0 22.9 0.5 H211 A:YSK303 0.3 23.2 0.5 C21 A:YSK303 1.4 19.4 0.5 C28 A:YSK303 1.4 22.1 0.5 C20 A:YSK303 2.3 18.4 0.5 H253 A:YSK303 2.3 25.3 0.5 C30 A:YSK303 2.4 20.5 0.5 C22 A:YSK303 2.4 23.4 0.5 H251 A:YSK303 2.4 35.2 0.5 C22 A:YSK303 2.4 20.0 0.5 H201 A:YSK303 2.5 22.0 0.5 H231 A:YSK303 2.5 31.9 0.5 H301 A:YSK303 2.6 24.6 0.5 HB2 A:HIS240 2.6 19.3 1.0 H231 A:YSK303 2.6 25.2 0.5 O A:HOH487 2.7 16.9 0.6 C23 A:YSK303 2.9 26.6 0.5 C23 A:YSK303 3.0 21.0 0.5 C25 A:YSK303 3.2 29.4 0.5 O A:HOH519 3.2 10.5 0.6 C25 A:YSK303 3.2 21.1 0.5 O A:HOH627 3.2 22.6 0.6 HD1 A:HIS201 3.2 25.0 0.7 H252 A:YSK303 3.3 35.2 0.5 CB A:HIS240 3.4 16.1 1.0 HB3 A:HIS240 3.4 19.3 1.0 H251 A:YSK303 3.5 25.3 0.5 HE1 A:HIS201 3.5 25.9 0.7 C19 A:YSK303 3.6 18.1 0.5 C19 A:YSK303 3.7 19.4 0.5 C28 A:YSK303 3.7 20.0 0.5 C21 A:YSK303 3.7 21.7 0.5 S24 A:YSK303 3.7 29.2 0.5 S24 A:YSK303 3.8 21.4 0.5 ND1 A:HIS201 3.9 20.8 0.7 H232 A:YSK303 3.9 31.9 0.5 CG A:HIS240 3.9 16.1 1.0 H232 A:YSK303 4.0 25.2 0.5 CE1 A:HIS201 4.0 21.6 0.7 H252 A:YSK303 4.1 25.3 0.5 C30 A:YSK303 4.1 19.4 0.5 H253 A:YSK303 4.1 35.2 0.5 C20 A:YSK303 4.2 20.9 0.5 HD2 A:HIS240 4.2 18.4 1.0 CD2 A:HIS240 4.3 15.3 1.0 O16 A:YSK303 4.3 18.2 0.5 O A:HIS240 4.4 15.3 1.0 HA2 A:GLY209 4.5 28.8 1.0 ND1 A:HIS201 4.5 20.6 0.3 HA3 A:GLY209 4.5 28.8 1.0 H211 A:YSK303 4.5 26.0 0.5 O A:HOH476 4.6 12.4 0.7 HE1 A:HIS201 4.6 25.5 0.3 O A:HOH669 4.6 24.1 0.4 CA A:HIS240 4.6 14.5 1.0 O26 A:YSK303 4.7 21.3 0.5 C A:HIS240 4.7 14.8 1.0 O27 A:YSK303 4.7 29.5 0.5 O26 A:YSK303 4.8 29.9 0.5 C18 A:YSK303 4.8 16.6 0.5 ND1 A:HIS240 4.8 15.0 1.0 F29 A:YSK303 4.8 21.1 0.5 C15 A:YSK303 4.8 17.4 0.5 O16 A:YSK303 4.8 14.7 0.5 O27 A:YSK303 4.8 22.2 0.5 CE1 A:HIS201 4.9 21.2 0.3 C18 A:YSK303 4.9 17.3 0.5 HG2 A:GLU202 5.0 19.4 1.0 CA A:GLY209 5.0 24.0 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 2850 To Be Published.