Magnesium in PDB 9uet: Cryo-Em Structure of Human Choline-Phosphotransferase 1

All present enzymatic activity of Cryo-Em Structure of Human Choline-Phosphotransferase 1:
2.7.8.2;

The binding sites of Magnesium atom in the Cryo-Em Structure of Human Choline-Phosphotransferase 1 (pdb code 9uet). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryo-Em Structure of Human Choline-Phosphotransferase 1, PDB code: 9uet:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Cryo-Em Structure of Human Choline-Phosphotransferase 1


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 Human Choline-Phosphotransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:30.0 occ:1.00 OD2 A:ASP132 1.7 82.5 1.0 O13 A:POV501 2.0 79.2 1.0 OD2 A:ASP136 2.4 71.4 1.0 OD2 A:ASP111 2.4 87.5 1.0 CG A:ASP132 2.5 82.5 1.0 P A:POV501 2.6 79.2 1.0 OD1 A:ASP111 2.7 87.5 1.0 OD1 A:ASP132 2.7 82.5 1.0 O11 A:POV501 2.8 79.2 1.0 CG A:ASP111 2.8 87.5 1.0 O12 A:POV501 2.9 79.2 1.0 MG A:MG503 3.1 30.0 1.0 CG A:ASP136 3.3 71.4 1.0 OD1 A:ASP136 3.6 71.4 1.0 C11 A:POV501 3.7 79.2 1.0 CB A:ASP132 3.8 82.5 1.0 C1 A:POV501 3.9 79.2 1.0 O14 A:POV501 4.0 79.2 1.0 CB A:ASP111 4.3 87.5 1.0 O A:ASP132 4.5 82.5 1.0 CB A:ASP136 4.7 71.4 1.0 CA A:ASP132 4.8 82.5 1.0 C A:ASP132 4.9 82.5 1.0 O A:ASP111 5.0 87.5 1.0

Magnesium binding site 2 out of 4 in the Cryo-Em Structure of Human Choline-Phosphotransferase 1


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 Human Choline-Phosphotransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:30.0 occ:1.00 OD1 A:ASP111 1.5 87.5 1.0 OD1 A:ASP114 2.1 98.4 1.0 OD2 A:ASP132 2.3 82.5 1.0 CG A:ASP132 2.5 82.5 1.0 OD2 A:ASP114 2.6 98.4 1.0 OD1 A:ASP132 2.7 82.5 1.0 CG A:ASP114 2.7 98.4 1.0 CG A:ASP111 2.7 87.5 1.0 MG A:MG502 3.1 30.0 1.0 O A:ASP111 3.1 87.5 1.0 CB A:ASP132 3.4 82.5 1.0 OD2 A:ASP111 3.5 87.5 1.0 CA A:ASP111 3.6 87.5 1.0 C A:ASP111 3.7 87.5 1.0 CB A:ASP111 3.7 87.5 1.0 N A:GLY115 4.2 104.9 1.0 CB A:ASP114 4.2 98.4 1.0 O13 A:POV501 4.5 79.2 1.0 CA A:ASP132 4.5 82.5 1.0 OD2 A:ASP136 4.7 71.4 1.0 CA A:GLY115 4.7 104.9 1.0 C A:ASP114 4.8 98.4 1.0 N A:ALA112 5.0 95.9 1.0 CA A:ASP114 5.0 98.4 1.0 OD1 A:ASP136 5.0 71.4 1.0

Magnesium binding site 3 out of 4 in the Cryo-Em Structure of Human Choline-Phosphotransferase 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryo-Em Structure of Human Choline-Phosphotransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:30.0 occ:1.00 OD2 B:ASP132 1.7 82.5 1.0 O13 B:POV501 2.0 79.2 1.0 OD2 B:ASP136 2.4 71.4 1.0 OD2 B:ASP111 2.4 87.5 1.0 CG B:ASP132 2.5 82.5 1.0 P B:POV501 2.6 79.2 1.0 OD1 B:ASP111 2.7 87.5 1.0 OD1 B:ASP132 2.7 82.5 1.0 O11 B:POV501 2.8 79.2 1.0 CG B:ASP111 2.8 87.5 1.0 O12 B:POV501 2.9 79.2 1.0 MG B:MG503 3.1 30.0 1.0 CG B:ASP136 3.3 71.4 1.0 OD1 B:ASP136 3.6 71.4 1.0 C11 B:POV501 3.7 79.2 1.0 CB B:ASP132 3.8 82.5 1.0 C1 B:POV501 3.9 79.2 1.0 O14 B:POV501 4.0 79.2 1.0 CB B:ASP111 4.3 87.5 1.0 O B:ASP132 4.5 82.5 1.0 CB B:ASP136 4.7 71.4 1.0 CA B:ASP132 4.8 82.5 1.0 C B:ASP132 4.9 82.5 1.0 O B:ASP111 5.0 87.5 1.0

Magnesium binding site 4 out of 4 in the Cryo-Em Structure of Human Choline-Phosphotransferase 1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryo-Em Structure of Human Choline-Phosphotransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:30.0 occ:1.00 OD1 B:ASP111 1.5 87.5 1.0 OD1 B:ASP114 2.1 98.4 1.0 OD2 B:ASP132 2.3 82.5 1.0 CG B:ASP132 2.5 82.5 1.0 OD2 B:ASP114 2.6 98.4 1.0 OD1 B:ASP132 2.7 82.5 1.0 CG B:ASP114 2.7 98.4 1.0 CG B:ASP111 2.7 87.5 1.0 MG B:MG502 3.1 30.0 1.0 O B:ASP111 3.1 87.5 1.0 CB B:ASP132 3.4 82.5 1.0 OD2 B:ASP111 3.5 87.5 1.0 CA B:ASP111 3.6 87.5 1.0 C B:ASP111 3.7 87.5 1.0 CB B:ASP111 3.7 87.5 1.0 N B:GLY115 4.2 104.9 1.0 CB B:ASP114 4.2 98.4 1.0 O13 B:POV501 4.5 79.2 1.0 CA B:ASP132 4.5 82.5 1.0 OD2 B:ASP136 4.7 71.4 1.0 CA B:GLY115 4.7 104.9 1.0 C B:ASP114 4.8 98.4 1.0 N B:ALA112 5.0 95.9 1.0 CA B:ASP114 5.0 98.4 1.0 OD1 B:ASP136 5.0 71.4 1.0

Y.L.He, H.W.Qian. Cryo-Em Structure of Human Choline-Phosphotransferase 1 To Be Published.