Manganese in PDB 9ere: SLFN11 Dimer Bound to Trna-Leu-Taa
Other elements in 9ere:
The structure of SLFN11 Dimer Bound to Trna-Leu-Taa also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the SLFN11 Dimer Bound to Trna-Leu-Taa
(pdb code 9ere). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the
SLFN11 Dimer Bound to Trna-Leu-Taa, PDB code: 9ere:
Jump to Manganese binding site number:
1;
2;
3;
Manganese binding site 1 out
of 3 in 9ere
Go back to
Manganese Binding Sites List in 9ere
Manganese binding site 1 out
of 3 in the SLFN11 Dimer Bound to Trna-Leu-Taa
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of SLFN11 Dimer Bound to Trna-Leu-Taa within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn1002
b:42.9
occ:1.00
|
OE2
|
A:GLU214
|
1.9
|
33.6
|
1.0
|
OD2
|
A:ASP252
|
1.9
|
41.6
|
1.0
|
OE2
|
A:GLU209
|
2.1
|
42.0
|
1.0
|
O
|
A:PHE215
|
2.3
|
35.3
|
1.0
|
CD
|
A:GLU214
|
3.0
|
28.0
|
1.0
|
CD
|
A:GLU209
|
3.2
|
33.9
|
1.0
|
OP1
|
T:U65
|
3.2
|
45.5
|
1.0
|
CG
|
A:ASP252
|
3.2
|
41.0
|
1.0
|
C
|
A:PHE215
|
3.4
|
33.3
|
1.0
|
CE
|
A:LYS216
|
3.5
|
39.9
|
1.0
|
OE1
|
A:GLU209
|
3.6
|
40.9
|
1.0
|
N
|
A:PHE215
|
3.7
|
30.2
|
1.0
|
OE1
|
A:GLU214
|
3.8
|
32.8
|
1.0
|
CG
|
A:GLU214
|
3.9
|
22.1
|
1.0
|
OD1
|
A:ASP252
|
4.0
|
41.8
|
1.0
|
CA
|
A:PHE215
|
4.0
|
28.9
|
1.0
|
CB
|
A:ASP252
|
4.1
|
41.4
|
1.0
|
OP2
|
T:C66
|
4.1
|
41.3
|
1.0
|
NZ
|
A:LYS216
|
4.2
|
40.0
|
1.0
|
N
|
A:LYS216
|
4.4
|
32.4
|
1.0
|
CB
|
A:PHE215
|
4.4
|
31.2
|
1.0
|
CG
|
A:GLU209
|
4.4
|
28.0
|
1.0
|
P
|
T:U65
|
4.5
|
45.5
|
1.0
|
C
|
A:GLU214
|
4.7
|
28.8
|
1.0
|
C5'
|
T:U65
|
4.7
|
37.1
|
1.0
|
O5'
|
T:U65
|
4.7
|
40.4
|
1.0
|
CD
|
A:LYS216
|
4.7
|
32.4
|
1.0
|
CA
|
A:LYS216
|
4.8
|
28.1
|
1.0
|
CA
|
A:ASP252
|
4.9
|
43.7
|
1.0
|
CG
|
A:LYS216
|
4.9
|
34.1
|
1.0
|
CA
|
A:GLU214
|
4.9
|
24.7
|
1.0
|
|
Manganese binding site 2 out
of 3 in 9ere
Go back to
Manganese Binding Sites List in 9ere
Manganese binding site 2 out
of 3 in the SLFN11 Dimer Bound to Trna-Leu-Taa
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of SLFN11 Dimer Bound to Trna-Leu-Taa within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1002
b:39.2
occ:1.00
|
OE2
|
B:GLU214
|
2.1
|
42.5
|
1.0
|
OP1
|
U:C77
|
2.1
|
71.2
|
1.0
|
OD2
|
B:ASP252
|
2.1
|
59.1
|
1.0
|
OE2
|
B:GLU209
|
2.2
|
38.9
|
1.0
|
O
|
B:PHE215
|
2.3
|
41.4
|
1.0
|
CD
|
B:GLU209
|
3.1
|
32.5
|
1.0
|
CD
|
B:GLU214
|
3.2
|
36.9
|
1.0
|
OE1
|
B:GLU209
|
3.3
|
33.5
|
1.0
|
MN
|
B:MN1003
|
3.3
|
69.9
|
1.0
|
CG
|
B:ASP252
|
3.3
|
60.9
|
1.0
|
C
|
B:PHE215
|
3.4
|
36.9
|
1.0
|
P
|
U:C77
|
3.5
|
78.9
|
1.0
|
N
|
B:PHE215
|
3.8
|
35.6
|
1.0
|
CE
|
B:LYS216
|
3.9
|
45.1
|
1.0
|
CG
|
B:GLU214
|
4.0
|
27.8
|
1.0
|
CA
|
B:PHE215
|
4.1
|
32.9
|
1.0
|
OE1
|
B:GLU214
|
4.1
|
38.3
|
1.0
|
CB
|
B:ASP252
|
4.2
|
61.2
|
1.0
|
OD1
|
B:ASP252
|
4.2
|
59.3
|
1.0
|
OP2
|
U:C77
|
4.2
|
70.3
|
1.0
|
CD
|
B:LYS216
|
4.4
|
46.0
|
1.0
|
CB
|
B:PHE215
|
4.4
|
39.1
|
1.0
|
CG
|
B:GLU209
|
4.5
|
30.0
|
1.0
|
N
|
B:LYS216
|
4.5
|
45.0
|
1.0
|
O5'
|
U:C77
|
4.5
|
75.5
|
1.0
|
C5'
|
U:C77
|
4.5
|
72.5
|
1.0
|
CG
|
B:LYS216
|
4.7
|
41.3
|
1.0
|
CA
|
B:LYS216
|
4.8
|
43.2
|
1.0
|
NZ
|
B:LYS216
|
4.8
|
45.7
|
1.0
|
C
|
B:GLU214
|
4.8
|
32.7
|
1.0
|
|
Manganese binding site 3 out
of 3 in 9ere
Go back to
Manganese Binding Sites List in 9ere
Manganese binding site 3 out
of 3 in the SLFN11 Dimer Bound to Trna-Leu-Taa
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of SLFN11 Dimer Bound to Trna-Leu-Taa within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn1003
b:69.9
occ:1.00
|
OE2
|
B:GLU214
|
2.4
|
42.5
|
1.0
|
OE1
|
B:GLU209
|
2.6
|
33.5
|
1.0
|
OE1
|
B:GLU214
|
2.6
|
38.3
|
1.0
|
CD
|
B:GLU214
|
2.9
|
36.9
|
1.0
|
O
|
B:THR138
|
2.9
|
28.4
|
1.0
|
MN
|
B:MN1002
|
3.3
|
39.2
|
1.0
|
CD
|
B:GLU209
|
3.4
|
32.5
|
1.0
|
OE2
|
B:GLU209
|
3.7
|
38.9
|
1.0
|
C
|
B:THR138
|
4.2
|
23.5
|
1.0
|
OP1
|
U:C77
|
4.2
|
71.2
|
1.0
|
NH1
|
B:ARG135
|
4.3
|
27.9
|
1.0
|
OD2
|
B:ASP252
|
4.4
|
59.1
|
1.0
|
CG
|
B:GLU214
|
4.4
|
27.8
|
1.0
|
NH2
|
B:ARG135
|
4.5
|
23.9
|
1.0
|
OP2
|
U:C77
|
4.5
|
70.3
|
1.0
|
CG
|
B:GLU209
|
4.7
|
30.0
|
1.0
|
CB
|
B:THR138
|
4.8
|
26.6
|
1.0
|
OH
|
B:TYR234
|
4.8
|
40.7
|
1.0
|
CB
|
B:GLU209
|
4.8
|
28.2
|
1.0
|
CZ
|
B:ARG135
|
4.8
|
20.9
|
1.0
|
P
|
U:C77
|
4.9
|
78.9
|
1.0
|
CA
|
B:THR138
|
4.9
|
17.9
|
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 11:29:47 2024
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