Magnesium in PDB 5mm9: Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding

The structure of Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding, PDB code: 5mm9 was solved by S.Skagseth, S.Akhter, M.H.Paulsen, O.Samuelsen, Z.Muhammad, H.-K.S.Leiros, A.Bayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.109, 79.070, 67.471, 90.00, 130.26, 90.00
R / Rfree (%)	15.7 / 20.1

The structure of Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding also contains other interesting chemical elements:

Zinc

(Zn)

6 atoms

The binding sites of Magnesium atom in the Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding (pdb code 5mm9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding, PDB code: 5mm9:

Magnesium binding site 1 out of 1 in the Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Vim-2_2B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:20.0 occ:1.00 H B:CYS221 2.3 14.7 1.0 HA3 B:GLY220 2.6 16.7 1.0 O B:HOH577 2.7 14.6 1.0 OG1 B:THR115 2.7 11.7 1.0 ND1 B:HIS116 2.7 9.4 1.0 N B:CYS221 3.1 12.3 1.0 HE1 B:HIS116 3.1 14.6 1.0 HD2 B:ARG121 3.2 13.9 1.0 CE1 B:HIS116 3.3 12.1 1.0 HB B:THR115 3.3 11.3 1.0 HG1 B:THR115 3.3 14.0 1.0 CA B:GLY220 3.5 13.9 1.0 CB B:THR115 3.6 9.5 1.0 HB2 B:CYS221 3.6 16.1 1.0 C B:GLY220 3.8 14.2 1.0 HA2 B:GLY220 3.8 16.7 1.0 CG B:HIS116 4.0 8.3 1.0 H B:ALA222 4.0 16.0 1.0 HB2 B:ASN200 4.0 12.9 1.0 C B:THR115 4.0 12.3 1.0 O B:THR115 4.1 13.1 1.0 HB3 B:HIS116 4.1 12.8 1.0 HG3 B:ARG121 4.1 15.8 1.0 CD B:ARG121 4.1 11.6 1.0 CB B:CYS221 4.1 13.4 1.0 CA B:CYS221 4.1 10.7 1.0 SG B:CYS221 4.2 12.9 1.0 O B:LEU201 4.2 11.4 1.0 HB3 B:ASN200 4.3 12.9 1.0 N B:HIS116 4.3 10.0 1.0 CA B:THR115 4.5 8.8 1.0 H B:LEU201 4.5 13.0 1.0 H B:HIS116 4.5 12.0 1.0 O B:GLY219 4.5 13.3 1.0 CB B:HIS116 4.5 10.7 1.0 NE2 B:HIS116 4.5 10.8 1.0 N B:GLY220 4.6 12.8 1.0 CB B:ASN200 4.6 10.8 1.0 HG21 B:THR115 4.6 15.4 1.0 HD3 B:ARG121 4.7 13.9 1.0 OD2 B:ASP84 4.7 12.1 1.0 N B:ALA222 4.7 13.3 1.0 CG B:ARG121 4.7 13.2 1.0 HH11 B:ARG121 4.7 19.2 1.0 NE B:ARG121 4.7 14.9 1.0 HA B:ASN200 4.7 13.3 1.0 CG2 B:THR115 4.7 12.8 1.0 HE2 B:TYR218 4.8 13.7 1.0 CD2 B:HIS116 4.9 9.2 1.0 HA B:CYS221 4.9 12.9 1.0 C B:CYS221 4.9 11.8 1.0 O B:GLY220 4.9 12.8 1.0 H B:THR115 4.9 12.7 1.0 HH B:TYR218 5.0 22.6 1.0

S.Skagseth, S.Akhter, M.H.Paulsen, Z.Muhammad, S.Lauksund, H.S.Leiros, A.Bayer. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding. Eur J Med Chem V. 135 159 2017.
ISSN: ISSN 1768-3254
PubMed: 28445786
DOI: 10.1016/J.EJMECH.2017.04.035