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
Go back to
Magnesium Binding Sites List in 8urp
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
Go back to
Magnesium Binding Sites List in 8urp
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
Go back to
Magnesium Binding Sites List in 8urp
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
Go back to
Magnesium Binding Sites List in 8urp
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
|