Magnesium in PDB 8pu1: Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp

The structure of Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp, PDB code: 8pu1 was solved by A.Garcia-Pino, A.Talavera Perez, L.Dominguez Molina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.26 / 1.70
Space group	F 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	227.81, 227.81, 227.81, 90, 90, 90
R / Rfree (%)	22.4 / 24.6

The structure of Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp also contains other interesting chemical elements:

Arsenic

(As)

1 atom

The binding sites of Magnesium atom in the Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp (pdb code 8pu1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp, PDB code: 8pu1:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg106 b:85.0 occ:1.00 O1G B:APC306 2.5 84.1 0.7 O B:HOH407 3.0 56.0 1.0 O B:HOH593 3.0 75.5 1.0 O B:HOH610 3.2 72.7 1.0 O A:HOH263 3.5 59.4 1.0 C2 A:POL105 3.5 77.9 1.0 O A:HOH203 3.6 43.1 1.0 CD1 A:PHE11 3.6 45.1 1.0 PG B:APC306 3.6 83.9 0.7 CE1 A:PHE11 3.8 46.4 1.0 C3 A:POL105 3.9 77.9 1.0 O2G B:APC306 3.9 83.9 0.7 O B:HOH527 3.9 84.8 1.0 O B:HOH571 4.1 82.7 1.0 OE1 A:GLN43 4.2 48.4 1.0 O3G B:APC306 4.3 83.8 0.7 C1 A:POL105 4.7 77.9 1.0 O B:HOH496 4.9 90.4 1.0 CG A:PHE11 4.9 42.9 1.0 O3B B:APC306 4.9 83.7 0.7 O A:POL105 4.9 77.9 1.0 CD A:GLN43 5.0 45.7 1.0 OG B:SER70 5.0 36.9 1.0 NE2 A:GLN43 5.0 46.6 1.0

Magnesium binding site 2 out of 3 in the Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:56.4 occ:1.00 O B:HOH530 2.3 48.7 1.0 OD1 B:ASP90 3.0 36.7 1.0 CB B:LYS66 3.4 32.4 1.0 CD B:LYS66 3.6 45.2 1.0 CE B:LYS66 3.6 49.8 1.0 CG B:ASP90 3.9 36.2 1.0 CB B:SER70 3.9 34.4 1.0 CG B:LYS66 4.0 38.7 1.0 OD2 B:ASP90 4.1 40.8 1.0 CD B:LYS74 4.2 47.6 1.0 NZ B:LYS66 4.3 51.6 1.0 O B:HOH420 4.4 71.9 1.0 CE B:LYS74 4.4 52.5 1.0 N B:ALA71 4.4 31.8 1.0 O B:ASP90 4.6 29.2 1.0 C B:SER70 4.6 32.6 1.0 O B:SER67 4.6 29.9 1.0 C B:ASP90 4.7 29.4 1.0 CA B:ALA71 4.7 31.5 1.0 CA B:LYS66 4.7 28.5 1.0 N B:ILE91 4.8 27.6 1.0 OG B:SER70 4.8 36.9 1.0 CA B:ILE91 4.9 28.2 1.0 CG1 B:ILE91 4.9 29.7 1.0 CA B:SER70 4.9 32.5 1.0 CB B:ALA71 5.0 31.6 1.0

Magnesium binding site 3 out of 3 in the Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:85.5 occ:1.00 O B:HOH440 2.3 74.2 1.0 O B:HOH602 2.5 56.7 1.0 O1B B:APC306 2.5 83.3 0.7 O B:HOH496 2.9 90.4 1.0 NH1 B:ARG77 3.8 66.6 1.0 PB B:APC306 3.8 83.3 0.7 O B:HOH565 3.8 65.7 1.0 OH B:TYR78 4.1 49.4 1.0 O B:HOH420 4.1 71.9 1.0 CG B:LYS74 4.1 41.4 1.0 C3A B:APC306 4.3 83.1 0.7 CE2 B:TYR78 4.3 45.1 1.0 CE B:LYS74 4.4 52.5 1.0 O3B B:APC306 4.5 83.7 0.7 CZ B:ARG77 4.5 66.3 1.0 CD B:ARG77 4.5 54.9 1.0 O B:HOH597 4.6 75.4 1.0 CZ B:TYR78 4.7 46.8 1.0 NZ B:LYS74 4.7 55.5 1.0 NE B:ARG77 4.8 61.5 1.0 O B:HOH416 4.8 62.9 1.0 O2G B:APC306 4.9 83.9 0.7 CD B:LYS74 4.9 47.6 1.0

A.Garcia-Pino, A.Talavera Perez, L.Dominguez Molina. Structure of the Toxin/Antitoxin Complex Farel/ATFAREL2 with Apcpp To Be Published.