Fluorine in PDB 8b1z: Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56

The structure of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56, PDB code: 8b1z was solved by F.Vascon, L.Lazzarato, M.Bersani, E.Gianquinto, J.D.Docquier, F.Spyrakis, D.Tondi, L.Cendron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.19 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.61, 73.964, 77.115, 90, 90, 90
R / Rfree (%)	17.3 / 20.9

The structure of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Zinc	(Zn)	4 atoms

The binding sites of Fluorine atom in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 (pdb code 8b1z). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56, PDB code: 8b1z:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 within 5.0Å range: probe atom residue distance (Å) B Occ A:F304 b:30.7 occ:0.72 F1 A:ORL304 0.0 30.7 0.7 C14 A:ORL304 1.3 27.6 0.7 F2 A:ORL304 2.1 33.5 0.7 F3 A:ORL304 2.1 31.6 0.7 C13 A:ORL304 2.3 21.0 0.7 C15 A:ORL304 2.8 21.6 0.7 NE2 A:GLN123 3.1 21.8 0.5 C12 A:ORL304 3.5 20.2 0.7 CD2 A:LEU65 3.9 35.2 1.0 CD A:GLN123 4.1 21.7 0.5 C16 A:ORL304 4.2 18.5 0.7 OE1 A:GLN123 4.5 25.3 0.5 CG A:GLN123 4.5 20.3 0.5 CB A:GLN123 4.6 18.3 0.5 C11 A:ORL304 4.7 19.7 0.7 CZ3 A:TRP93 4.8 19.4 1.0 CB A:GLN123 4.9 19.0 0.5 C10 A:ORL304 4.9 17.2 0.7 C12 A:1PE306 5.0 47.8 1.0

Fluorine binding site 2 out of 6 in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 within 5.0Å range: probe atom residue distance (Å) B Occ A:F304 b:33.5 occ:0.72 F2 A:ORL304 0.0 33.5 0.7 C14 A:ORL304 1.3 27.6 0.7 F1 A:ORL304 2.1 30.7 0.7 F3 A:ORL304 2.1 31.6 0.7 C13 A:ORL304 2.3 21.0 0.7 C12 A:ORL304 2.7 20.2 0.7 C15 A:ORL304 3.6 21.6 0.7 CG A:MET67 3.7 53.4 1.0 CD2 A:LEU65 3.7 35.2 1.0 SD A:MET67 3.8 65.5 1.0 CE A:MET67 3.9 71.0 1.0 C11 A:ORL304 4.1 19.7 0.7 C12 A:1PE306 4.2 47.8 1.0 OH2 A:1PE306 4.3 51.8 1.0 C16 A:ORL304 4.7 18.5 0.7 CG A:LEU65 4.8 34.5 1.0 CZ3 A:TRP93 4.8 19.4 1.0 C10 A:ORL304 4.9 17.2 0.7

Fluorine binding site 3 out of 6 in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 within 5.0Å range: probe atom residue distance (Å) B Occ A:F304 b:31.6 occ:0.72 F3 A:ORL304 0.0 31.6 0.7 C14 A:ORL304 1.3 27.6 0.7 F1 A:ORL304 2.1 30.7 0.7 F2 A:ORL304 2.1 33.5 0.7 C13 A:ORL304 2.3 21.0 0.7 C15 A:ORL304 3.1 21.6 0.7 C12 A:ORL304 3.2 20.2 0.7 C16 A:ORL304 4.4 18.5 0.7 C11 A:ORL304 4.5 19.7 0.7 CE A:MET67 4.8 71.0 1.0 OH2 A:1PE306 4.9 51.8 1.0 NE2 A:GLN123 4.9 21.8 0.5 C10 A:ORL304 4.9 17.2 0.7

Fluorine binding site 4 out of 6 in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 within 5.0Å range: probe atom residue distance (Å) B Occ B:F303 b:35.7 occ:0.82 F1 B:ORL303 0.0 35.7 0.8 C14 B:ORL303 1.3 30.2 0.8 F3 B:ORL303 2.1 36.0 0.8 F2 B:ORL303 2.1 33.1 0.8 C13 B:ORL303 2.3 23.3 0.8 C12 B:ORL303 2.7 23.6 0.8 C15 B:ORL303 3.6 21.5 0.8 CE B:MET67 3.7 58.4 1.0 CG B:MET67 3.7 50.0 1.0 SD B:MET67 3.8 64.0 1.0 C11 B:ORL303 4.1 20.4 0.8 CD2 B:LEU65 4.3 28.9 1.0 C16 B:ORL303 4.7 18.8 0.8 CB B:MET67 4.8 45.2 1.0 C10 B:ORL303 4.9 18.7 0.8

Fluorine binding site 5 out of 6 in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 within 5.0Å range: probe atom residue distance (Å) B Occ B:F303 b:33.1 occ:0.82 F2 B:ORL303 0.0 33.1 0.8 C14 B:ORL303 1.3 30.2 0.8 F3 B:ORL303 2.1 36.0 0.8 F1 B:ORL303 2.1 35.7 0.8 C13 B:ORL303 2.3 23.3 0.8 C15 B:ORL303 2.9 21.5 0.8 C12 B:ORL303 3.4 23.6 0.8 C16 B:ORL303 4.2 18.8 0.8 OE1 B:GLN123 4.3 19.5 0.6 O B:HOH421 4.3 34.6 1.0 C11 B:ORL303 4.6 20.4 0.8 C10 B:ORL303 4.9 18.7 0.8

Fluorine binding site 6 out of 6 in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56 within 5.0Å range: probe atom residue distance (Å) B Occ B:F303 b:36.0 occ:0.82 F3 B:ORL303 0.0 36.0 0.8 C14 B:ORL303 1.3 30.2 0.8 F2 B:ORL303 2.1 33.1 0.8 F1 B:ORL303 2.1 35.7 0.8 C13 B:ORL303 2.3 23.3 0.8 C15 B:ORL303 3.0 21.5 0.8 OE1 B:GLN123 3.2 19.5 0.6 CD2 B:LEU65 3.3 28.9 1.0 C12 B:ORL303 3.3 23.6 0.8 CD B:GLN123 4.0 18.6 0.6 C16 B:ORL303 4.3 18.8 0.8 NE2 B:GLN123 4.5 20.1 0.6 CG B:GLN123 4.5 20.0 0.4 CZ3 B:TRP93 4.5 18.5 1.0 C11 B:ORL303 4.5 20.4 0.8 O B:HOH421 4.6 34.6 1.0 CB B:GLN123 4.7 18.9 0.4 CG B:LEU65 4.7 26.4 1.0 CE3 B:TRP93 4.7 16.9 1.0 C10 B:ORL303 4.9 18.7 0.8 CB B:GLN123 5.0 17.9 0.6

F.Vascon, L.Lazzarato, M.Bersani, E.Gianquinto, J.D.Docquier, F.Spyrakis, D.Tondi, L.Cendron. Structural Characterization of Triazole-Based Inhibitors of Metallo-Beta-Lactamases To Be Published.