Fluorine in PDB 7uyb: Inhibitor Bound VIM1

The structure of Inhibitor Bound VIM1, PDB code: 7uyb was solved by T.O.Fischmann, G.Scapin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	16.25 / 1.11
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.601, 67.812, 40.177, 90, 91.61, 90
R / Rfree (%)	15.6 / 16.6

The structure of Inhibitor Bound VIM1 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Fluorine atom in the Inhibitor Bound VIM1 (pdb code 7uyb). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Inhibitor Bound VIM1, PDB code: 7uyb:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Inhibitor Bound VIM1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Inhibitor Bound VIM1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:14.2 occ:1.00 F2 A:OK0303 0.0 14.2 1.0 C16 A:OK0303 1.3 11.9 1.0 F1 A:OK0303 2.1 14.8 1.0 F A:OK0303 2.2 11.6 1.0 C15 A:OK0303 2.4 13.6 1.0 O1 A:OK0303 2.6 11.7 1.0 C17 A:OK0303 3.2 16.3 1.0 O A:HOH554 3.3 16.8 1.0 C14 A:OK0303 3.3 11.4 1.0 CE1 A:PHE62 3.5 20.9 1.0 S A:OK0303 3.6 10.0 1.0 CZ A:PHE62 3.7 21.1 1.0 O A:HOH639 3.8 8.1 1.0 CD1 A:PHE62 4.0 18.4 1.0 O A:HOH714 4.1 25.6 1.0 CE2 A:PHE62 4.4 23.1 1.0 O A:HOH446 4.5 13.2 1.0 C18 A:OK0303 4.6 15.9 1.0 N5 A:OK0303 4.6 9.3 1.0 C12 A:OK0303 4.6 11.2 1.0 N A:ASP117 4.6 9.0 1.0 O A:OK0303 4.6 10.9 1.0 CB A:ASP117 4.7 12.0 1.0 CB A:HIS116 4.7 8.7 1.0 CG A:PHE62 4.7 16.2 1.0 CD2 A:PHE62 4.9 18.9 1.0

Fluorine binding site 2 out of 3 in the Inhibitor Bound VIM1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Inhibitor Bound VIM1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:11.6 occ:1.00 F A:OK0303 0.0 11.6 1.0 C16 A:OK0303 1.4 11.9 1.0 F1 A:OK0303 2.1 14.8 1.0 F2 A:OK0303 2.2 14.2 1.0 C15 A:OK0303 2.4 13.6 1.0 O1 A:OK0303 2.6 11.7 1.0 C14 A:OK0303 2.9 11.4 1.0 S A:OK0303 3.1 10.0 1.0 OD1 A:ASP118 3.1 9.3 1.0 N A:ASP118 3.3 9.1 1.0 N5 A:OK0303 3.3 9.3 1.0 CG A:ASP118 3.3 9.0 1.0 C17 A:OK0303 3.5 16.3 1.0 N A:ASP117 3.6 9.0 1.0 CB A:ASP118 3.7 9.7 1.0 CB A:HIS116 3.7 8.7 1.0 OD2 A:ASP118 3.8 10.3 1.0 C A:ASP117 4.1 10.4 1.0 CA A:ASP118 4.1 9.0 1.0 CA A:ASP117 4.1 9.7 1.0 CB A:ASP117 4.2 12.0 1.0 C12 A:OK0303 4.3 11.2 1.0 C A:HIS116 4.3 8.4 1.0 NE1 A:TRP87 4.4 10.8 1.0 O A:HOH639 4.4 8.1 1.0 O A:OK0303 4.5 10.9 1.0 CE2 A:TRP87 4.5 11.4 1.0 O A:HOH554 4.5 16.8 1.0 CZ2 A:TRP87 4.6 13.3 1.0 CA A:HIS116 4.6 8.5 1.0 CG A:HIS116 4.6 9.4 1.0 C18 A:OK0303 4.7 15.9 1.0 O A:HOH446 4.9 13.2 1.0 ZN A:ZN301 4.9 9.3 1.0

Fluorine binding site 3 out of 3 in the Inhibitor Bound VIM1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Inhibitor Bound VIM1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F303 b:14.8 occ:1.00 F1 A:OK0303 0.0 14.8 1.0 C16 A:OK0303 1.3 11.9 1.0 F2 A:OK0303 2.1 14.2 1.0 F A:OK0303 2.1 11.6 1.0 C15 A:OK0303 2.4 13.6 1.0 C17 A:OK0303 2.7 16.3 1.0 CZ2 A:TRP87 3.0 13.3 1.0 NE1 A:TRP87 3.2 10.8 1.0 CE2 A:TRP87 3.3 11.4 1.0 O A:HOH446 3.3 13.2 1.0 CD1 A:PHE62 3.5 18.4 1.0 C14 A:OK0303 3.7 11.4 1.0 CE1 A:PHE62 3.7 20.9 1.0 C18 A:OK0303 4.0 15.9 1.0 CH2 A:TRP87 4.1 15.3 1.0 O1 A:OK0303 4.1 11.7 1.0 CG A:PHE62 4.1 16.2 1.0 CB A:ASP117 4.3 12.0 1.0 N A:ASP118 4.3 9.1 1.0 CD1 A:TRP87 4.4 10.8 1.0 CZ A:PHE62 4.4 21.1 1.0 CD2 A:TRP87 4.5 9.0 1.0 S A:OK0303 4.6 10.0 1.0 CB A:ASP118 4.6 9.7 1.0 CD2 A:PHE62 4.7 18.9 1.0 CG A:ASP118 4.7 9.0 1.0 CB A:PHE62 4.7 15.7 1.0 C12 A:OK0303 4.7 11.2 1.0 CE2 A:PHE62 4.8 23.1 1.0 C A:ASP117 4.9 10.4 1.0 N A:ASP117 4.9 9.0 1.0 CA A:ASP117 4.9 9.7 1.0 C11 A:OK0303 4.9 13.2 1.0 OD1 A:ASP118 4.9 9.3 1.0 CA A:ASP118 5.0 9.0 1.0 CG A:TRP87 5.0 8.9 1.0 OD2 A:ASP117 5.0 18.0 1.0

T.O.Fischmann, G.Scapin. Inhibitor Bound VIM1 To Be Published.