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Magnesium in PDB 5nhz: Vim-2_10B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding

Protein crystallography data

The structure of Vim-2_10B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding, PDB code: 5nhz was solved by S.Skagseth, S.Akhter, M.H.Paulsen, O.Samuelsen, Z.Muhammad, K.-K.S.Leiros, A.Bayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.75 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.779, 90.872, 124.075, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 20.4

Other elements in 5nhz:

The structure of Vim-2_10B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding also contains other interesting chemical elements:

Zinc (Zn) 5 atoms
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Vim-2_10B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding (pdb code 5nhz). 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_10B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding, PDB code: 5nhz:

Magnesium binding site 1 out of 1 in 5nhz

Go back to Magnesium Binding Sites List in 5nhz
Magnesium binding site 1 out of 1 in the Vim-2_10B. 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_10B. Metallo-Beta-Lactamase Inhibitors By Bioisosteric Replacement: Preparation, Activity and Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg408

b:0.6
occ:1.00
OE2 B:GLU188 4.7 40.0 1.0

Reference:

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
Page generated: Mon Dec 14 20:55:45 2020

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