Magnesium in PDB 8ero: Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp

Enzymatic activity of Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp

All present enzymatic activity of Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp:
2.7.8.2;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp (pdb code 8ero). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp, PDB code: 8ero:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 8ero

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Magnesium binding site 1 out of 4 in the Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:64.7
occ:1.00
OD1 A:ASP132 2.0 78.8 1.0
OD1 A:ASP136 2.1 67.8 1.0
OD2 A:ASP111 2.2 80.0 1.0
CG A:ASP136 2.9 67.8 1.0
CG A:ASP111 3.0 80.0 1.0
OD2 A:ASP136 3.1 67.8 1.0
CG A:ASP132 3.2 78.8 1.0
OD1 A:ASP111 3.3 80.0 1.0
O A:ASP132 3.6 78.8 1.0
OD2 A:ASP132 3.8 78.8 1.0
OH A:TYR107 3.9 68.8 1.0
MG A:MG502 4.0 82.5 1.0
CB A:ASP111 4.3 80.0 1.0
C A:ASP132 4.3 78.8 1.0
CB A:ASP136 4.3 67.8 1.0
CB A:ASP132 4.3 78.8 1.0
CA A:ASP132 4.4 78.8 1.0
N A:ASP136 4.7 67.8 1.0
CZ A:TYR107 4.7 68.8 1.0
O1B A:CDP513 4.7 93.4 1.0
CA A:ASP136 4.8 67.8 1.0

Magnesium binding site 2 out of 4 in 8ero

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Magnesium binding site 2 out of 4 in the Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:82.5
occ:1.00
O1A A:CDP513 2.0 93.4 1.0
OD2 A:ASP132 2.2 78.8 1.0
OD1 A:ASP111 2.2 80.0 1.0
CG A:ASP132 3.1 78.8 1.0
O1B A:CDP513 3.2 93.4 1.0
OD1 A:ASP132 3.3 78.8 1.0
O A:ASP111 3.3 80.0 1.0
CG A:ASP111 3.4 80.0 1.0
PA A:CDP513 3.4 93.4 1.0
OD1 A:ASP114 3.6 86.6 1.0
O5' A:CDP513 4.0 93.4 1.0
OD2 A:ASP111 4.0 80.0 1.0
MG A:MG501 4.0 64.7 1.0
C A:ASP111 4.1 80.0 1.0
O3A A:CDP513 4.2 93.4 1.0
CA A:GLY115 4.3 93.5 1.0
N A:GLY115 4.3 93.5 1.0
CA A:ASP111 4.3 80.0 1.0
PB A:CDP513 4.4 93.4 1.0
CB A:ASP111 4.4 80.0 1.0
CB A:ASP132 4.4 78.8 1.0
O2A A:CDP513 4.5 93.4 1.0
CG A:ASP114 4.6 86.6 1.0
C6 A:CDP513 4.6 93.4 1.0
C5 A:CDP513 4.7 93.4 1.0
OD2 A:ASP114 4.8 86.6 1.0

Magnesium binding site 3 out of 4 in 8ero

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Magnesium binding site 3 out of 4 in the Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg504

b:65.6
occ:1.00
OD1 B:ASP132 2.0 79.1 1.0
OD1 B:ASP136 2.1 68.1 1.0
OD2 B:ASP111 2.2 80.1 1.0
CG B:ASP136 2.9 68.1 1.0
CG B:ASP111 3.0 80.1 1.0
OD2 B:ASP136 3.1 68.1 1.0
CG B:ASP132 3.2 79.1 1.0
OD1 B:ASP111 3.3 80.1 1.0
O B:ASP132 3.6 79.1 1.0
OD2 B:ASP132 3.8 79.1 1.0
OH B:TYR107 3.9 68.8 1.0
MG B:MG505 4.0 82.7 1.0
CB B:ASP111 4.3 80.1 1.0
C B:ASP132 4.3 79.1 1.0
CB B:ASP136 4.3 68.1 1.0
CB B:ASP132 4.3 79.1 1.0
CA B:ASP132 4.4 79.1 1.0
N B:ASP136 4.7 68.1 1.0
CZ B:TYR107 4.7 68.8 1.0
O1B B:CDP516 4.7 93.8 1.0
CA B:ASP136 4.8 68.1 1.0

Magnesium binding site 4 out of 4 in 8ero

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Magnesium binding site 4 out of 4 in the Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Xenopus CHOLINEPHOSPHOTRANSFERASE1 in Complex with Cdp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg505

b:82.7
occ:1.00
O1A B:CDP516 2.0 93.8 1.0
OD1 B:ASP111 2.2 80.1 1.0
OD2 B:ASP132 2.2 79.1 1.0
CG B:ASP132 3.1 79.1 1.0
O1B B:CDP516 3.2 93.8 1.0
OD1 B:ASP132 3.3 79.1 1.0
O B:ASP111 3.3 80.1 1.0
CG B:ASP111 3.4 80.1 1.0
PA B:CDP516 3.4 93.8 1.0
OD1 B:ASP114 3.6 86.6 1.0
O5' B:CDP516 4.0 93.8 1.0
OD2 B:ASP111 4.0 80.1 1.0
MG B:MG504 4.0 65.6 1.0
C B:ASP111 4.1 80.1 1.0
O3A B:CDP516 4.2 93.8 1.0
CA B:GLY115 4.3 93.5 1.0
N B:GLY115 4.3 93.5 1.0
CA B:ASP111 4.3 80.1 1.0
PB B:CDP516 4.4 93.8 1.0
CB B:ASP111 4.4 80.1 1.0
CB B:ASP132 4.4 79.1 1.0
O2A B:CDP516 4.5 93.8 1.0
CG B:ASP114 4.6 86.6 1.0
C6 B:CDP516 4.6 93.8 1.0
C5 B:CDP516 4.7 93.8 1.0
OD2 B:ASP114 4.8 86.6 1.0

Reference:

W.Lie, Z.Ming. Substrate Recognition and Catalysis in Eukaryotic Cholinephosphotransferase-1 To Be Published.
Page generated: Thu Jul 27 23:41:41 2023

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