Magnesium in PDB 8gyw: Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline

Enzymatic activity of Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline (pdb code 8gyw). 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) Complexed with Cdp-Choline, PDB code: 8gyw:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 8gyw

Go back to Magnesium Binding Sites List in 8gyw
Magnesium binding site 1 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline


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) Complexed with Cdp-Choline within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:135.0
occ:1.00
 O B:ASP133 2.3 137.7 1.0
O2B B:CDC503 2.6 141.5 1.0
O2A B:CDC503 2.9 141.5 1.0
OD1 B:ASP133 3.0 137.7 1.0
OD1 B:ASP136 3.0 145.9 1.0
OD2 B:ASP136 3.0 145.9 1.0
CG B:ASP136 3.2 145.9 1.0
C B:ASP133 3.3 137.7 1.0
OD2 B:ASP154 3.4 123.5 1.0
MG B:MG502 3.5 136.8 1.0
CG B:ASP133 3.7 137.7 1.0
PB B:CDC503 3.8 141.5 1.0
O3A B:CDC503 4.0 141.5 1.0
PA B:CDC503 4.0 141.5 1.0
N B:ALA134 4.1 144.7 1.0
CA B:ASP133 4.1 137.7 1.0
OD1 B:ASP154 4.1 123.5 1.0
CG B:ASP154 4.1 123.5 1.0
N B:GLY137 4.2 148.9 1.0
CA B:ALA134 4.2 144.7 1.0
OD2 B:ASP133 4.3 137.7 1.0
C5' B:CDC503 4.4 141.5 1.0
CB B:ASP133 4.5 137.7 1.0
O1B B:CDC503 4.5 141.5 1.0
CB B:ASP136 4.5 145.9 1.0
C B:ALA134 4.6 144.7 1.0
N B:ASP136 4.6 145.9 1.0
C15 B:CDC503 4.7 141.5 1.0
O5' B:CDC503 4.7 141.5 1.0
O B:ALA134 4.9 144.7 1.0
C14 B:CDC503 4.9 141.5 1.0
CA B:GLY137 4.9 148.9 1.0
CA B:ASP136 4.9 145.9 1.0

Magnesium binding site 2 out of 4 in 8gyw

Go back to Magnesium Binding Sites List in 8gyw
Magnesium binding site 2 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline


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) Complexed with Cdp-Choline within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:136.8
occ:1.00
 OD1 B:ASP154 2.0 123.5 1.0
O2B B:CDC503 2.1 141.5 1.0
OD1 B:ASP158 2.5 115.3 1.0
OD2 B:ASP133 2.6 137.7 1.0
OD1 B:ASP133 2.6 137.7 1.0
CG B:ASP154 2.9 123.5 1.0
CG B:ASP133 3.0 137.7 1.0
OD2 B:ASP154 3.1 123.5 1.0
PB B:CDC503 3.2 141.5 1.0
CG B:ASP158 3.3 115.3 1.0
MG B:MG501 3.5 135.0 1.0
O3B B:CDC503 3.5 141.5 1.0
OD2 B:ASP158 3.5 115.3 1.0
C14 B:CDC503 4.2 141.5 1.0
O1B B:CDC503 4.3 141.5 1.0
CB B:ASP154 4.4 123.5 1.0
O B:ASP154 4.4 123.5 1.0
O3A B:CDC503 4.5 141.5 1.0
CB B:ASP133 4.5 137.7 1.0
C B:ASP154 4.6 123.5 1.0
CB B:ASP158 4.7 115.3 1.0
OD2 B:ASP136 4.7 145.9 1.0
C15 B:CDC503 4.8 141.5 1.0
CA B:ASP154 4.9 123.5 1.0
O B:ASP133 4.9 137.7 1.0
ND1 B:HIS155 5.0 120.8 1.0

Magnesium binding site 3 out of 4 in 8gyw

Go back to Magnesium Binding Sites List in 8gyw
Magnesium binding site 3 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline


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) Complexed with Cdp-Choline within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:135.0
occ:1.00
 O A:ASP133 2.3 137.7 1.0
O2B A:CDC503 2.6 141.5 1.0
O2A A:CDC503 2.9 141.5 1.0
OD1 A:ASP133 3.0 137.7 1.0
OD1 A:ASP136 3.0 145.9 1.0
OD2 A:ASP136 3.0 145.9 1.0
CG A:ASP136 3.2 145.9 1.0
C A:ASP133 3.3 137.7 1.0
OD2 A:ASP154 3.4 123.5 1.0
MG A:MG502 3.5 136.8 1.0
CG A:ASP133 3.7 137.7 1.0
PB A:CDC503 3.8 141.5 1.0
O3A A:CDC503 4.0 141.5 1.0
PA A:CDC503 4.0 141.5 1.0
N A:ALA134 4.1 144.7 1.0
CA A:ASP133 4.1 137.7 1.0
CG A:ASP154 4.1 123.5 1.0
OD1 A:ASP154 4.1 123.5 1.0
N A:GLY137 4.2 148.9 1.0
CA A:ALA134 4.2 144.7 1.0
OD2 A:ASP133 4.3 137.7 1.0
C5' A:CDC503 4.4 141.5 1.0
CB A:ASP133 4.5 137.7 1.0
O1B A:CDC503 4.5 141.5 1.0
CB A:ASP136 4.5 145.9 1.0
C A:ALA134 4.6 144.7 1.0
N A:ASP136 4.6 145.9 1.0
C15 A:CDC503 4.7 141.5 1.0
O5' A:CDC503 4.7 141.5 1.0
O A:ALA134 4.9 144.7 1.0
C14 A:CDC503 4.9 141.5 1.0
CA A:GLY137 4.9 148.9 1.0
CA A:ASP136 4.9 145.9 1.0

Magnesium binding site 4 out of 4 in 8gyw

Go back to Magnesium Binding Sites List in 8gyw
Magnesium binding site 4 out of 4 in the Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase (CEPT1) Complexed with Cdp-Choline


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) Complexed with Cdp-Choline within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:136.8
occ:1.00
 OD1 A:ASP154 2.0 123.5 1.0
O2B A:CDC503 2.1 141.5 1.0
OD1 A:ASP158 2.5 115.3 1.0
OD2 A:ASP133 2.6 137.7 1.0
OD1 A:ASP133 2.6 137.7 1.0
CG A:ASP154 2.9 123.5 1.0
CG A:ASP133 3.0 137.7 1.0
OD2 A:ASP154 3.1 123.5 1.0
PB A:CDC503 3.2 141.5 1.0
CG A:ASP158 3.3 115.3 1.0
MG A:MG501 3.5 135.0 1.0
O3B A:CDC503 3.5 141.5 1.0
OD2 A:ASP158 3.5 115.3 1.0
C14 A:CDC503 4.2 141.5 1.0
O1B A:CDC503 4.3 141.5 1.0
CB A:ASP154 4.4 123.5 1.0
O A:ASP154 4.4 123.5 1.0
O3A A:CDC503 4.5 141.5 1.0
CB A:ASP133 4.5 137.7 1.0
C A:ASP154 4.6 123.5 1.0
CB A:ASP158 4.7 115.3 1.0
OD2 A:ASP136 4.7 145.9 1.0
C15 A:CDC503 4.8 141.5 1.0
CA A:ASP154 4.9 123.5 1.0
O A:ASP133 4.9 137.7 1.0
ND1 A:HIS155 5.0 120.8 1.0

Reference:

H.W.Qian, Z.H.Wang. Structural Basis For Catalysis of Human Choline/Ethanolamine Phosphotransferase in the Kennedy Pathway To Be Published.
Page generated: Tue Apr 11 16:14:24 2023

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