Magnesium in PDB 5hev: Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium

The structure of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium, PDB code: 5hev was solved by M.Davlieva, Y.Shamoo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.02 / 3.19
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	68.032, 68.032, 276.949, 90.00, 90.00, 120.00
R / Rfree (%)	21.9 / 27

The structure of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium also contains other interesting chemical elements:

Fluorine

(F)

12 atoms

The binding sites of Magnesium atom in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium (pdb code 5hev). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium, PDB code: 5hev:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:29.2 occ:1.00 OD2 A:ASP54 1.9 40.5 1.0 F1 A:BEF302 1.9 40.1 1.0 O A:VAL56 2.0 28.5 1.0 OD1 A:ASP9 2.0 47.9 1.0 CG A:ASP9 3.0 39.6 1.0 CG A:ASP54 3.0 31.7 1.0 BE A:BEF302 3.2 32.6 1.0 C A:VAL56 3.2 30.0 1.0 OD2 A:ASP9 3.3 49.9 1.0 OD1 A:ASP8 3.3 36.8 1.0 OD1 A:ASP54 3.5 34.4 1.0 CG A:MET57 3.7 33.3 1.0 F3 A:BEF302 4.0 34.3 1.0 N A:MET57 4.1 27.2 1.0 CB A:ASP54 4.2 30.0 1.0 CA A:VAL56 4.2 35.6 1.0 CA A:MET57 4.2 32.9 1.0 N A:ASP9 4.3 39.6 1.0 CB A:ASP9 4.3 34.7 1.0 N A:VAL56 4.4 25.4 1.0 CG A:ASP8 4.4 28.9 1.0 CB A:VAL56 4.4 26.7 1.0 F2 A:BEF302 4.4 27.9 1.0 CB A:MET57 4.6 47.9 1.0 NZ A:LYS104 4.7 38.2 1.0 CG1 A:VAL56 4.7 13.0 1.0 CA A:ASP9 4.8 42.3 1.0 OD2 A:ASP8 4.9 39.6 1.0 CD2 A:HIS10 4.9 50.8 1.0 NE2 A:HIS10 4.9 46.3 1.0 N A:HIS10 5.0 33.0 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg301 b:40.2 occ:1.00 OD2 F:ASP54 1.8 44.4 1.0 F3 F:BEF302 1.9 36.1 1.0 OD1 F:ASP9 1.9 48.1 1.0 O F:VAL56 2.0 48.7 1.0 CG F:ASP9 2.8 39.6 1.0 BE F:BEF302 2.8 53.3 1.0 CG F:ASP54 2.9 48.6 1.0 OD1 F:ASP8 3.1 46.5 1.0 OD2 F:ASP9 3.2 34.9 1.0 C F:VAL56 3.3 40.3 1.0 CG F:MET57 3.6 35.4 1.0 F1 F:BEF302 3.7 46.5 1.0 OD1 F:ASP54 3.7 56.4 1.0 N F:ASP9 3.9 37.9 1.0 CB F:ASP54 3.9 40.3 1.0 F2 F:BEF302 4.0 51.1 1.0 CB F:ASP9 4.0 35.4 1.0 N F:MET57 4.2 45.5 1.0 CA F:VAL56 4.2 35.5 1.0 CA F:MET57 4.3 47.8 1.0 CG F:ASP8 4.3 47.6 1.0 N F:VAL56 4.4 35.0 1.0 CB F:VAL56 4.4 28.9 1.0 CA F:ASP9 4.4 31.0 1.0 NE2 F:HIS10 4.5 51.5 1.0 CB F:MET57 4.5 40.1 1.0 CD2 F:HIS10 4.5 48.8 1.0 CE1 F:HIS10 4.8 50.4 1.0 C F:ASP9 4.9 44.5 1.0 CG F:HIS10 4.9 43.2 1.0 CG1 F:VAL56 4.9 47.3 1.0 N F:HIS10 4.9 47.2 1.0 OD2 F:ASP8 4.9 51.1 1.0 SD F:MET57 5.0 41.0 1.0 C F:ASP8 5.0 35.9 1.0 ND1 F:HIS10 5.0 49.4 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:40.6 occ:1.00 OD2 B:ASP54 1.9 49.5 1.0 F1 B:BEF302 1.9 51.1 1.0 OD1 B:ASP9 2.0 47.9 1.0 O B:VAL56 2.0 44.8 1.0 CG B:ASP9 2.7 53.1 1.0 OD2 B:ASP9 2.8 53.5 1.0 CG B:ASP54 3.0 46.1 1.0 BE B:BEF302 3.0 45.0 1.0 CG2 B:VAL56 3.2 44.9 1.0 C B:VAL56 3.2 35.3 1.0 OD1 B:ASP54 3.6 43.8 1.0 OD1 B:ASP8 3.7 47.6 1.0 F2 B:BEF302 3.8 31.4 1.0 CA B:VAL56 3.9 42.5 1.0 N B:VAL56 4.0 35.6 1.0 CB B:VAL56 4.0 34.4 1.0 CB B:ASP9 4.1 38.8 1.0 CB B:ASP54 4.2 38.6 1.0 CG B:MET57 4.2 40.6 1.0 N B:MET57 4.3 38.5 1.0 F3 B:BEF302 4.3 41.4 1.0 N B:ASP9 4.5 46.9 1.0 CA B:MET57 4.6 44.0 1.0 NE2 B:HIS10 4.6 41.2 1.0 CD2 B:HIS10 4.7 42.3 1.0 CA B:ASP9 4.9 36.3 1.0 CG B:ASP8 4.9 42.0 1.0 C B:LEU55 5.0 33.9 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg301 b:36.7 occ:1.00 OD2 C:ASP54 1.7 51.4 1.0 F2 C:BEF302 1.8 34.6 1.0 OD1 C:ASP9 1.8 51.0 1.0 O C:VAL56 2.1 54.6 1.0 CG C:ASP9 2.8 44.0 1.0 BE C:BEF302 2.9 49.3 1.0 OD1 C:ASP8 2.9 43.8 1.0 CG C:ASP54 3.0 48.7 1.0 C C:VAL56 3.3 45.3 1.0 OD2 C:ASP9 3.3 40.5 1.0 OD1 C:ASP54 3.7 51.6 1.0 CG C:MET57 3.9 39.4 1.0 N C:ASP9 3.9 37.4 1.0 F1 C:BEF302 3.9 59.1 1.0 F3 C:BEF302 3.9 52.3 1.0 CB C:ASP54 4.0 39.7 1.0 CB C:ASP9 4.0 34.6 1.0 CG C:ASP8 4.1 43.0 1.0 N C:MET57 4.2 43.2 1.0 CA C:VAL56 4.2 33.3 1.0 CA C:MET57 4.3 38.6 1.0 CB C:VAL56 4.3 25.5 1.0 N C:VAL56 4.4 33.5 1.0 CA C:ASP9 4.5 34.0 1.0 NE2 C:HIS10 4.5 43.2 1.0 CD2 C:HIS10 4.6 37.3 1.0 OD2 C:ASP8 4.6 50.3 1.0 CB C:MET57 4.7 44.6 1.0 CE1 C:HIS10 4.7 48.9 1.0 CG C:HIS10 4.8 35.0 1.0 CG1 C:VAL56 4.8 21.7 1.0 ND1 C:HIS10 4.9 48.9 1.0 C C:ASP9 4.9 36.7 1.0 N C:HIS10 4.9 41.1 1.0 NZ C:LYS104 4.9 54.9 1.0 C C:ASP8 4.9 39.9 1.0 CA C:ASP8 5.0 43.1 1.0

M.Davlieva, A.Tovar-Yanez, K.Debruler, P.G.Leonard, M.R.Zianni, C.A.Arias, Y.Shamoo. An Adaptive Mutation in Enterococcus Faecium Liar Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes Liar in An Activated State. J.Mol.Biol. V. 428 4503 2016.
ISSN: ISSN 0022-2836
PubMed: 27670715
DOI: 10.1016/J.JMB.2016.09.016