Magnesium in PDB 9gmw: SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)
Other elements in 9gmw:
The structure of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)
(pdb code 9gmw). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State), PDB code: 9gmw:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 9gmw
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Magnesium Binding Sites List in 9gmw
Magnesium binding site 1 out
of 4 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Mg101
b:25.1
occ:1.00
|
OP1
|
T:C58
|
1.9
|
67.0
|
1.0
|
OP2
|
T:U60
|
1.9
|
51.5
|
1.0
|
P
|
T:U60
|
3.1
|
54.2
|
1.0
|
P
|
T:C58
|
3.3
|
62.6
|
1.0
|
O5'
|
T:U60
|
3.5
|
48.6
|
1.0
|
OP1
|
T:U60
|
3.9
|
45.2
|
1.0
|
O3'
|
T:G57
|
3.9
|
66.4
|
1.0
|
OP2
|
T:C58
|
4.2
|
52.2
|
1.0
|
C5
|
T:U60
|
4.2
|
42.1
|
1.0
|
OP2
|
T:G61
|
4.2
|
34.9
|
1.0
|
O5'
|
T:C58
|
4.3
|
59.7
|
1.0
|
O3'
|
T:G59
|
4.4
|
63.4
|
1.0
|
C6
|
T:U60
|
4.4
|
44.1
|
1.0
|
C5'
|
T:C58
|
4.5
|
59.4
|
1.0
|
C3'
|
T:G59
|
4.7
|
52.5
|
1.0
|
C3'
|
T:C58
|
4.9
|
57.8
|
1.0
|
C5'
|
T:U60
|
4.9
|
45.5
|
1.0
|
OP1
|
T:G59
|
5.0
|
59.4
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 9gmw
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Magnesium Binding Sites List in 9gmw
Magnesium binding site 2 out
of 4 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Mg102
b:31.8
occ:1.00
|
N7
|
T:G15
|
2.1
|
69.7
|
1.0
|
C8
|
T:G15
|
3.0
|
73.4
|
1.0
|
C5
|
T:G15
|
3.2
|
70.9
|
1.0
|
O6
|
T:G15
|
3.5
|
70.3
|
1.0
|
C6
|
T:G15
|
3.7
|
70.8
|
1.0
|
O4
|
T:U8
|
3.9
|
69.2
|
1.0
|
C4
|
T:U8
|
4.2
|
73.2
|
1.0
|
N9
|
T:G15
|
4.2
|
73.8
|
1.0
|
C4
|
T:G15
|
4.3
|
70.4
|
1.0
|
O4
|
T:U16
|
4.3
|
83.1
|
1.0
|
N3
|
T:U8
|
4.4
|
73.0
|
1.0
|
OP2
|
T:A14
|
4.5
|
86.3
|
1.0
|
OP2
|
T:G15
|
4.5
|
69.0
|
1.0
|
N7
|
T:A14
|
4.9
|
75.1
|
1.0
|
C5
|
T:U8
|
4.9
|
68.7
|
1.0
|
C8
|
T:A14
|
4.9
|
78.2
|
1.0
|
OP1
|
T:A7
|
5.0
|
74.8
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 9gmw
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Magnesium Binding Sites List in 9gmw
Magnesium binding site 3 out
of 4 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Mg103
b:30.1
occ:1.00
|
N7
|
T:G13
|
2.3
|
83.6
|
1.0
|
C8
|
T:G13
|
3.1
|
84.8
|
1.0
|
C5
|
T:G13
|
3.4
|
82.2
|
1.0
|
OP2
|
T:C12
|
3.7
|
94.1
|
1.0
|
O6
|
T:G13
|
3.8
|
78.0
|
1.0
|
C6
|
T:G13
|
4.0
|
79.5
|
1.0
|
OP2
|
T:G13
|
4.1
|
87.4
|
1.0
|
C5
|
T:U8
|
4.1
|
68.7
|
1.0
|
OP2
|
T:G9
|
4.2
|
78.9
|
1.0
|
N9
|
T:G13
|
4.4
|
82.8
|
1.0
|
OP2
|
T:U8
|
4.4
|
69.8
|
1.0
|
C6
|
T:U8
|
4.5
|
67.7
|
1.0
|
C4
|
T:G13
|
4.5
|
82.2
|
1.0
|
C5
|
T:C12
|
4.7
|
88.3
|
1.0
|
O5'
|
T:C12
|
4.8
|
101.2
|
1.0
|
C6
|
T:C12
|
4.8
|
91.2
|
1.0
|
P
|
T:C12
|
4.9
|
102.8
|
1.0
|
C4
|
T:U8
|
4.9
|
73.2
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 9gmw
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Magnesium Binding Sites List in 9gmw
Magnesium binding site 4 out
of 4 in the SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of SLFN11 Wt Dimer Bound to Trna-Leu-Taa (Pre-Cleavage State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
T:Mg104
b:27.5
occ:1.00
|
OP2
|
T:A69
|
2.3
|
59.3
|
1.0
|
P
|
T:A69
|
3.6
|
56.8
|
1.0
|
OP2
|
T:G57
|
3.9
|
63.1
|
1.0
|
N7
|
T:G57
|
4.1
|
59.8
|
1.0
|
OP1
|
T:A69
|
4.2
|
56.4
|
1.0
|
OP2
|
T:C56
|
4.3
|
71.9
|
1.0
|
OP1
|
T:A68
|
4.4
|
52.0
|
1.0
|
C3'
|
T:A68
|
4.4
|
50.4
|
1.0
|
O3'
|
T:A68
|
4.5
|
55.0
|
1.0
|
O5'
|
T:A69
|
4.7
|
52.8
|
1.0
|
C8
|
T:G57
|
4.7
|
56.1
|
1.0
|
|
Reference:
M.Kugler,
F.J.Metzner,
K.P.Hopfner,
K.Lammens.
Phosphorylation-Mediated Conformational Change Regulates Human SLFN11 Nat Commun 2024.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-024-54833-7
Page generated: Sun Dec 15 11:24:25 2024
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