Calcium 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:

Zinc	(Zn)	4 atoms
Fluorine	(F)	6 atoms

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Ndm-1 Metallo-Beta-Lactamase in Complex with Triazole-Based Inhibitor CP56, PDB code: 8b1z:

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


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca 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:Ca303 b:41.1 occ:1.00 OD2 A:ASP130 2.2 31.2 1.0 OD2 A:ASP95 2.3 29.4 1.0 O A:HOH448 2.6 21.9 1.0 CG A:ASP130 3.3 27.8 1.0 CG A:ASP95 3.3 28.0 1.0 OD1 A:ASP95 3.6 25.1 1.0 CB A:ASP130 3.7 24.8 1.0 O A:HOH463 4.2 31.9 1.0 O A:HOH445 4.3 26.8 1.0 OD1 A:ASP130 4.3 29.8 1.0 O A:GLY127 4.5 21.4 1.0 CB A:ASP95 4.7 22.9 1.0 N A:ASP130 4.7 20.6 1.0 O A:HOH432 4.8 20.8 1.0 CG2 A:VAL155 4.8 24.5 1.0 CA A:ASP130 4.9 23.8 1.0

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.