Magnesium in PDB 8gyx: Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1)

All present enzymatic activity of Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1):
2.7.8.1; 2.7.8.2; 2.7.8.22;

The binding sites of Magnesium atom in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) (pdb code 8gyx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1), PDB code: 8gyx:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:98.6 occ:1.00 OD1 B:ASP133 2.2 101.6 1.0 MG B:MG503 2.4 93.7 1.0 O B:ASP133 2.7 101.6 1.0 OD1 B:ASP154 2.8 94.0 1.0 C11 B:POV501 3.0 91.9 1.0 CG B:ASP133 3.0 101.6 1.0 OD1 B:ASP136 3.2 105.4 1.0 O12 B:POV501 3.4 91.9 1.0 C B:ASP133 3.4 101.6 1.0 OD2 B:ASP133 3.6 101.6 1.0 CG B:ASP154 3.7 94.0 1.0 OD2 B:ASP136 3.8 105.4 1.0 CG B:ASP136 3.8 105.4 1.0 OD2 B:ASP154 3.9 94.0 1.0 O13 B:POV501 3.9 91.9 1.0 CA B:ASP133 4.0 101.6 1.0 CB B:ASP133 4.1 101.6 1.0 N B:ALA134 4.2 105.9 1.0 C12 B:POV501 4.3 91.9 1.0 P B:POV501 4.4 91.9 1.0 CA B:ALA134 4.4 105.9 1.0 OD2 B:ASP158 4.6 90.6 1.0 CB B:ASP154 5.0 94.0 1.0

Magnesium binding site 2 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:93.7 occ:1.00 OD2 B:ASP158 2.2 90.6 1.0 MG B:MG502 2.4 98.6 1.0 OD1 B:ASP133 2.6 101.6 1.0 OD1 B:ASP154 2.7 94.0 1.0 OD2 B:ASP154 2.7 94.0 1.0 O12 B:POV501 2.7 91.9 1.0 O13 B:POV501 2.8 91.9 1.0 OD2 B:ASP133 2.9 101.6 1.0 CG B:ASP154 3.0 94.0 1.0 CG B:ASP133 3.1 101.6 1.0 CG B:ASP158 3.2 90.6 1.0 P B:POV501 3.2 91.9 1.0 C11 B:POV501 3.4 91.9 1.0 O11 B:POV501 3.5 91.9 1.0 OD1 B:ASP158 3.5 90.6 1.0 CB B:ASP154 4.5 94.0 1.0 CB B:ASP158 4.6 90.6 1.0 CB B:ASP133 4.6 101.6 1.0 O B:ASP154 4.7 94.0 1.0 O14 B:POV501 4.7 91.9 1.0 ND1 B:HIS155 4.8 91.0 1.0 C12 B:POV501 4.8 91.9 1.0 O B:ASP133 4.8 101.6 1.0 C B:ASP154 4.9 94.0 1.0 C1 B:POV501 4.9 91.9 1.0 C3 B:POV501 4.9 91.9 1.0

Magnesium binding site 3 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:98.6 occ:1.00 OD1 A:ASP133 2.2 101.6 1.0 MG A:MG503 2.4 93.7 1.0 O A:ASP133 2.7 101.6 1.0 OD1 A:ASP154 2.8 94.0 1.0 C11 A:POV501 3.0 91.9 1.0 CG A:ASP133 3.0 101.6 1.0 OD1 A:ASP136 3.2 105.4 1.0 O12 A:POV501 3.4 91.9 1.0 C A:ASP133 3.4 101.6 1.0 OD2 A:ASP133 3.6 101.6 1.0 CG A:ASP154 3.7 94.0 1.0 OD2 A:ASP136 3.8 105.4 1.0 CG A:ASP136 3.8 105.4 1.0 OD2 A:ASP154 3.9 94.0 1.0 O13 A:POV501 3.9 91.9 1.0 CA A:ASP133 4.0 101.6 1.0 CB A:ASP133 4.1 101.6 1.0 N A:ALA134 4.2 105.9 1.0 C12 A:POV501 4.3 91.9 1.0 P A:POV501 4.4 91.9 1.0 CA A:ALA134 4.4 105.9 1.0 OD2 A:ASP158 4.6 90.6 1.0 CB A:ASP154 5.0 94.0 1.0

Magnesium binding site 4 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg503 b:93.7 occ:1.00 OD2 A:ASP158 2.2 90.6 1.0 MG A:MG502 2.4 98.6 1.0 OD1 A:ASP133 2.6 101.6 1.0 OD1 A:ASP154 2.7 94.0 1.0 OD2 A:ASP154 2.7 94.0 1.0 O12 A:POV501 2.7 91.9 1.0 O13 A:POV501 2.8 91.9 1.0 OD2 A:ASP133 2.9 101.6 1.0 CG A:ASP154 3.0 94.0 1.0 CG A:ASP133 3.1 101.6 1.0 P A:POV501 3.2 91.9 1.0 CG A:ASP158 3.2 90.6 1.0 C11 A:POV501 3.4 91.9 1.0 O11 A:POV501 3.5 91.9 1.0 OD1 A:ASP158 3.5 90.6 1.0 CB A:ASP154 4.5 94.0 1.0 CB A:ASP158 4.6 90.6 1.0 CB A:ASP133 4.6 101.6 1.0 O A:ASP154 4.7 94.0 1.0 O14 A:POV501 4.7 91.9 1.0 ND1 A:HIS155 4.8 91.0 1.0 C12 A:POV501 4.8 91.9 1.0 O A:ASP133 4.8 101.6 1.0 C A:ASP154 4.9 94.0 1.0 C1 A:POV501 4.9 91.9 1.0 C3 A:POV501 4.9 91.9 1.0

H.W.Qian, Z.H.Wang. Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase in the Kennedy Pathway To Be Published.