Fluorine in PDB 8p93: Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2163

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2163, PDB code: 8p93 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)	34.48 / 1.13
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.43, 67.67, 40.15, 90, 93.42, 90
R / Rfree (%)	12.8 / 14.2

The structure of Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2163 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 2163 (pdb code 8p93). 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 2163, PDB code: 8p93:
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 2163


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 2163 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:17.6 occ:0.49 F28 A:XAQ303 0.0 17.6 0.5 H141 A:XAQ303 0.4 22.5 0.5 C27 A:XAQ303 1.3 16.1 0.5 C14 A:XAQ303 1.4 18.7 0.5 C15 A:XAQ303 2.3 16.4 0.5 C29 A:XAQ303 2.3 14.3 0.5 C13 A:XAQ303 2.4 18.0 0.5 H171 A:XAQ303 2.4 25.8 0.5 C15 A:XAQ303 2.5 20.0 0.5 H171 A:XAQ303 2.5 30.8 0.5 H131 A:XAQ303 2.6 21.6 0.5 H291 A:XAQ303 2.6 17.1 0.5 N17 A:XAQ303 2.7 21.5 0.5 HE1 A:TYR67 2.8 16.3 1.0 C16 A:XAQ303 2.8 19.0 0.5 H161 A:XAQ303 2.9 27.4 0.5 H161 A:XAQ303 2.9 22.8 0.5 N17 A:XAQ303 2.9 25.7 0.5 C16 A:XAQ303 2.9 22.8 0.5 O A:HOH535 2.9 47.5 1.0 HA2 A:GLY209 3.4 23.8 1.0 CE1 A:TYR67 3.6 13.6 1.0 C14 A:XAQ303 3.6 14.6 0.5 C12 A:XAQ303 3.6 13.4 0.5 C12 A:XAQ303 3.7 17.1 0.5 C27 A:XAQ303 3.8 19.2 0.5 H162 A:XAQ303 3.9 22.8 0.5 H162 A:XAQ303 4.0 27.4 0.5 HD1 A:TYR67 4.0 15.8 1.0 C13 A:XAQ303 4.1 13.7 0.5 S18 A:XAQ303 4.2 22.7 0.5 C29 A:XAQ303 4.2 17.7 0.5 O A:HOH663 4.2 28.6 1.0 CD1 A:TYR67 4.2 13.2 1.0 CA A:GLY209 4.3 19.9 1.0 H311 A:XAQ303 4.3 16.4 0.5 S18 A:XAQ303 4.4 28.0 0.5 H311 A:XAQ303 4.4 18.8 0.5 CZ A:TYR67 4.4 12.9 1.0 OH A:TYR67 4.4 14.4 1.0 O A:HOH618 4.4 45.4 1.0 H141 A:XAQ303 4.5 17.6 0.5 O19 A:XAQ303 4.5 29.8 0.5 O A:HOH479 4.5 27.3 0.7 C A:GLY209 4.6 19.3 1.0 O19 A:XAQ303 4.6 23.4 0.5 O20 A:XAQ303 4.6 22.1 0.5 HG A:SER207 4.7 37.3 1.0 HA3 A:GLY209 4.7 23.8 1.0 C11 A:XAQ303 4.8 12.8 0.5 C11 A:XAQ303 4.9 15.5 0.5 OG A:SER207 4.9 31.1 1.0 O A:GLY209 4.9 21.0 1.0 H A:GLY209 4.9 24.8 1.0 F28 A:XAQ303 4.9 20.3 0.5 N A:ASN210 4.9 18.3 1.0 O20 A:XAQ303 4.9 27.9 0.5

Fluorine binding site 2 out of 2 in the Crystal Structure of the Metallo-Beta-Lactamase VIM1 with 2163


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 2163 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:20.3 occ:0.51 F28 A:XAQ303 0.0 20.3 0.5 H141 A:XAQ303 0.6 17.6 0.5 C27 A:XAQ303 1.4 19.2 0.5 C14 A:XAQ303 1.6 14.6 0.5 C29 A:XAQ303 2.4 17.7 0.5 C13 A:XAQ303 2.4 13.7 0.5 C15 A:XAQ303 2.5 20.0 0.5 H162 A:XAQ303 2.5 27.4 0.5 H131 A:XAQ303 2.6 16.4 0.5 H291 A:XAQ303 2.6 21.3 0.5 C15 A:XAQ303 2.6 16.4 0.5 HB2 A:HIS240 2.6 16.1 1.0 H162 A:XAQ303 2.7 22.8 0.5 O A:HOH504 2.8 19.7 0.7 C16 A:XAQ303 3.0 22.8 0.5 C16 A:XAQ303 3.1 19.0 0.5 O A:HOH404 3.1 12.4 0.3 HB3 A:HIS240 3.3 16.1 1.0 CB A:HIS240 3.3 13.4 1.0 O A:HOH583 3.4 18.7 0.5 HE1 A:HIS201 3.5 18.1 0.6 HD1 A:HIS201 3.5 17.7 0.6 O A:HOH493 3.5 13.5 0.9 H161 A:XAQ303 3.7 22.8 0.5 O20 A:XAQ303 3.7 27.9 0.5 C12 A:XAQ303 3.7 17.1 0.5 H161 A:XAQ303 3.7 27.4 0.5 C14 A:XAQ303 3.7 18.7 0.5 C12 A:XAQ303 3.7 13.4 0.5 CG A:HIS240 3.8 12.2 1.0 C27 A:XAQ303 3.8 16.1 0.5 N17 A:XAQ303 4.0 25.7 0.5 ND1 A:HIS201 4.0 14.8 0.6 CE1 A:HIS201 4.0 15.1 0.6 O20 A:XAQ303 4.1 22.1 0.5 C13 A:XAQ303 4.2 18.0 0.5 CD2 A:HIS240 4.3 12.4 1.0 HD2 A:HIS240 4.3 14.9 1.0 C29 A:XAQ303 4.3 14.3 0.5 S18 A:XAQ303 4.3 28.0 0.5 HA2 A:GLY209 4.3 23.8 1.0 N17 A:XAQ303 4.4 21.5 0.5 HA3 A:GLY209 4.4 23.8 1.0 O10 A:XAQ303 4.5 14.6 0.5 H141 A:XAQ303 4.6 22.5 0.5 H211 A:XAQ303 4.6 28.9 0.5 ND1 A:HIS240 4.6 12.8 1.0 O A:HIS240 4.6 11.8 1.0 O A:HOH474 4.7 11.6 0.9 H211 A:XAQ303 4.7 32.8 0.5 CA A:HIS240 4.7 12.2 1.0 S18 A:XAQ303 4.8 22.7 0.5 CA A:GLY209 4.8 19.9 1.0 HD1 A:HIS240 4.8 15.4 1.0 O10 A:XAQ303 4.8 13.4 0.5 H171 A:XAQ303 4.9 30.8 0.5 C11 A:XAQ303 4.9 15.5 0.5 C A:HIS240 4.9 11.5 1.0 C11 A:XAQ303 4.9 12.8 0.5 F28 A:XAQ303 4.9 17.6 0.5 HD2 A:HIS201 4.9 22.4 0.4 O A:HOH632 5.0 37.4 0.7 O A:HOH515 5.0 10.3 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 2163 To Be Published.