Magnesium in PDB 8i6s: Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc

The binding sites of Magnesium atom in the Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc (pdb code 8i6s). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc, PDB code: 8i6s:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:132.2 occ:1.00 OG1 B:THR140 2.1 121.9 1.0 O3A D:ATP301 2.1 159.5 1.0 O2B D:ATP301 2.1 159.5 1.0 OG D:SER42 2.3 153.0 1.0 CB D:SER42 2.5 153.0 1.0 PB D:ATP301 2.5 159.5 1.0 CB B:THR140 2.8 121.9 1.0 N B:THR140 3.0 121.9 1.0 PA D:ATP301 3.4 159.5 1.0 CA B:THR140 3.5 121.9 1.0 O1B D:ATP301 3.5 159.5 1.0 O2A D:ATP301 3.5 159.5 1.0 O3B D:ATP301 3.8 159.5 1.0 O3G D:ATP301 3.8 159.5 1.0 CA D:SER42 3.8 153.0 1.0 O1A D:ATP301 3.9 159.5 1.0 N D:SER42 4.0 153.0 1.0 C B:SER139 4.1 142.5 1.0 CG2 B:THR140 4.1 121.9 1.0 CA B:SER139 4.3 142.5 1.0 PG D:ATP301 4.4 159.5 1.0 CB B:SER139 4.5 142.5 1.0 C B:THR140 4.7 121.9 1.0 C D:SER42 4.7 153.0 1.0 O5' D:ATP301 4.7 159.5 1.0 N B:GLY141 4.8 124.4 1.0 N D:THR43 5.0 172.0 1.0

Magnesium binding site 2 out of 2 in the Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of Pseudomonas Aeruginosa Ftse(E163Q)X/Envc Complex with Atp in Peptidisc within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg303 b:158.0 occ:1.00 O1A B:ATP302 2.1 169.1 1.0 O1B B:ATP302 2.3 169.1 1.0 N B:SER42 2.3 142.5 1.0 N B:LYS41 2.3 164.7 1.0 O3A B:ATP302 2.6 169.1 1.0 PB B:ATP302 2.8 169.1 1.0 PA B:ATP302 2.9 169.1 1.0 O B:ALA39 2.9 191.5 1.0 C B:GLY40 2.9 167.2 1.0 OG B:SER42 3.0 142.5 1.0 C B:LYS41 3.0 164.7 1.0 CA B:LYS41 3.1 164.7 1.0 CA B:GLY40 3.2 167.2 1.0 CG B:LYS41 3.2 164.7 1.0 CA B:SER42 3.3 142.5 1.0 CB B:SER42 3.5 142.5 1.0 O3B B:ATP302 3.7 169.1 1.0 CB B:LYS41 3.7 164.7 1.0 O2A B:ATP302 3.7 169.1 1.0 N B:THR43 3.7 153.5 1.0 C B:ALA39 3.8 191.5 1.0 O B:GLY40 3.8 167.2 1.0 NZ B:LYS41 3.9 164.7 1.0 N B:GLY40 4.0 167.2 1.0 O2B B:ATP302 4.1 169.1 1.0 C B:SER42 4.1 142.5 1.0 O5' B:ATP302 4.1 169.1 1.0 O B:LYS41 4.3 164.7 1.0 CD B:LYS41 4.4 164.7 1.0 CE B:LYS41 4.6 164.7 1.0 OG1 B:THR43 4.7 153.5 1.0 CA B:THR43 5.0 153.5 1.0 C5' B:ATP302 5.0 169.1 1.0

X.Xu, J.Li, W.Z.Chua, M.A.Pages, J.Shi, J.A.Hermoso, T.Bernhardt, L.T.Sham, M.Luo. Mechanistic Insights Into the Regulation of Cell Wall Hydrolysis By Ftsex and Envc at the Bacterial Division Site. Proc.Natl.Acad.Sci.Usa V. 120 97120 2023.
ISSN: ESSN 1091-6490
PubMed: 37186861
DOI: 10.1073/PNAS.2301897120