Magnesium in PDB 8urp: Membrane Protein Enzyme in State 2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Membrane Protein Enzyme in State 2 (pdb code 8urp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Membrane Protein Enzyme in State 2, PDB code: 8urp:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 8urp

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Magnesium binding site 1 out of 4 in the Membrane Protein Enzyme in State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Membrane Protein Enzyme in State 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:60.1
occ:1.00
OD2 A:ASP117 2.1 53.1 1.0
O2A A:CDC1005 2.1 70.8 1.0
O3B A:CDC1005 2.2 69.6 1.0
O A:ASP96 2.5 64.0 1.0
OD1 A:ASP99 2.6 74.1 1.0
OD1 A:ASP96 2.6 70.7 1.0
CG A:ASP117 3.1 61.5 1.0
OD2 A:ASP99 3.3 65.8 1.0
CG A:ASP99 3.3 67.9 1.0
PA A:CDC1005 3.4 77.2 1.0
OD1 A:ASP117 3.5 69.1 1.0
PB A:CDC1005 3.5 78.9 1.0
C A:ASP96 3.6 64.2 1.0
MG A:MG1002 3.6 73.5 1.0
CG A:ASP96 3.7 65.4 1.0
O3A A:CDC1005 3.9 72.7 1.0
CA A:ASP96 4.1 58.7 1.0
C5' A:CDC1005 4.2 68.5 1.0
O5' A:CDC1005 4.3 67.2 1.0
N A:GLY100 4.3 71.6 1.0
O1B A:CDC1005 4.4 76.3 1.0
C6 A:CDC1005 4.4 68.8 1.0
CB A:ASP117 4.4 52.6 1.0
C14 A:CDC1005 4.4 69.8 1.0
O1A A:CDC1005 4.5 75.5 1.0
C5 A:CDC1005 4.5 64.9 1.0
OD2 A:ASP96 4.6 68.2 1.0
CB A:ASP96 4.6 57.9 1.0
O2B A:CDC1005 4.6 71.6 1.0
N A:ALA97 4.8 73.4 1.0
CB A:ASP99 4.8 61.7 1.0
CA A:GLY100 4.8 67.0 1.0

Magnesium binding site 2 out of 4 in 8urp

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Magnesium binding site 2 out of 4 in the Membrane Protein Enzyme in State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Membrane Protein Enzyme in State 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:73.5
occ:1.00
OD2 A:ASP121 2.0 68.5 1.0
OD1 A:ASP117 2.1 69.1 1.0
OD1 A:ASP96 2.2 70.7 1.0
OD1 A:ASP121 2.6 64.1 1.0
CG A:ASP121 2.6 67.6 1.0
OD2 A:ASP96 2.7 68.2 1.0
CG A:ASP96 2.7 65.4 1.0
CG A:ASP117 3.1 61.5 1.0
O3B A:CDC1005 3.3 69.6 1.0
OD2 A:ASP117 3.4 53.1 1.0
MG A:MG1001 3.6 60.1 1.0
O A:ASP117 3.9 60.2 1.0
CB A:ASP121 4.1 58.0 1.0
CB A:ASP96 4.1 57.9 1.0
O A:HOH1101 4.2 74.5 1.0
CB A:ASP117 4.4 52.6 1.0
C A:ASP117 4.5 55.5 1.0
PB A:CDC1005 4.5 78.9 1.0
O1B A:CDC1005 4.7 76.3 1.0
OH A:TYR92 4.7 58.3 1.0
O A:ASP96 4.8 64.0 1.0
O32 A:PCF1006 4.8 83.2 1.0
CA A:ASP117 4.8 51.6 1.0
CA A:ASP96 4.8 58.7 1.0
O2B A:CDC1005 4.9 71.6 1.0

Magnesium binding site 3 out of 4 in 8urp

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Magnesium binding site 3 out of 4 in the Membrane Protein Enzyme in State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Membrane Protein Enzyme in State 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:46.8
occ:1.00
O1A B:CDC405 2.1 58.1 1.0
OD2 B:ASP117 2.1 50.3 1.0
O B:ASP96 2.2 55.8 1.0
OD1 B:ASP99 2.3 68.5 1.0
OD1 B:ASP96 2.4 67.6 1.0
O3B B:CDC405 2.7 63.5 1.0
OD2 B:ASP99 3.0 53.1 1.0
CG B:ASP99 3.0 56.4 1.0
CG B:ASP117 3.1 56.6 1.0
C B:ASP96 3.2 55.0 1.0
OD1 B:ASP117 3.3 60.3 1.0
PA B:CDC405 3.5 66.2 1.0
CG B:ASP96 3.5 59.8 1.0
CA B:ASP96 3.7 49.0 1.0
MG B:MG403 3.8 67.0 1.0
PB B:CDC405 3.9 75.7 1.0
O3A B:CDC405 4.1 63.4 1.0
CB B:ASP96 4.2 49.3 1.0
N B:GLY100 4.2 62.0 1.0
O5' B:CDC405 4.4 67.5 1.0
N B:ALA97 4.4 62.0 1.0
OD2 B:ASP96 4.4 64.4 1.0
O2A B:CDC405 4.5 66.4 1.0
CB B:ASP99 4.5 46.4 1.0
CB B:ASP117 4.5 45.1 1.0
C5 B:CDC405 4.5 55.1 1.0
O1B B:CDC405 4.6 68.2 1.0
C6 B:CDC405 4.6 58.2 1.0
C5' B:CDC405 4.8 62.4 1.0
CA B:ALA97 4.8 51.6 1.0
O B:PHE95 4.8 58.7 1.0
CA B:GLY100 4.9 57.0 1.0
N B:ASP99 4.9 57.4 1.0

Magnesium binding site 4 out of 4 in 8urp

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Magnesium binding site 4 out of 4 in the Membrane Protein Enzyme in State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Membrane Protein Enzyme in State 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:67.0
occ:1.00
OD2 B:ASP121 2.0 66.0 1.0
OD1 B:ASP96 2.2 67.6 1.0
OD1 B:ASP117 2.2 60.3 1.0
CG B:ASP121 2.7 67.0 1.0
OD1 B:ASP121 2.7 65.7 1.0
OD2 B:ASP96 2.7 64.4 1.0
CG B:ASP96 2.7 59.8 1.0
O3B B:CDC405 3.2 63.5 1.0
CG B:ASP117 3.3 56.6 1.0
O B:ASP117 3.3 59.3 1.0
MG B:MG402 3.8 46.8 1.0
OD2 B:ASP117 3.8 50.3 1.0
CB B:ASP96 4.1 49.3 1.0
CB B:ASP121 4.2 55.6 1.0
C B:ASP117 4.2 53.2 1.0
PB B:CDC405 4.5 75.7 1.0
CB B:ASP117 4.5 45.1 1.0
CA B:ASP117 4.6 40.8 1.0
OH B:TYR92 4.7 60.4 1.0
O2B B:CDC405 4.8 65.9 1.0
O B:ASP96 4.8 55.8 1.0
CA B:ASP96 4.9 49.0 1.0
O1B B:CDC405 5.0 68.2 1.0

Reference:

J.R.Roberts, Y.Horibata, F.Kwarcinski, V.Lam, A.M.Raczkowski, A.Hubbard, H.Sugimoto, G.G.Tall, M.D.Ohi, S.Maeda. Structural Basis For Catalysis and Selectivity of Phospholipid Synthesis By Eukaryotic Choline-Phosphotransferase To Be Published.
Page generated: Wed Nov 13 12:04:16 2024

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