Magnesium in PDB 8j0s: Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
Enzymatic activity of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
All present enzymatic activity of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq):
7.1.2.2;
Other elements in 8j0s:
The structure of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
(pdb code 8j0s). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the
Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq), PDB code: 8j0s:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
Magnesium binding site 1 out
of 5 in 8j0s
Go back to
Magnesium Binding Sites List in 8j0s
Magnesium binding site 1 out
of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg601
b:11.5
occ:1.00
|
O1B
|
A:ATP600
|
2.0
|
5.3
|
1.0
|
OG1
|
A:THR179
|
2.0
|
12.9
|
1.0
|
O1G
|
A:ATP600
|
2.3
|
5.3
|
1.0
|
PB
|
A:ATP600
|
3.3
|
5.3
|
1.0
|
CB
|
A:THR179
|
3.3
|
12.9
|
1.0
|
PG
|
A:ATP600
|
3.3
|
5.3
|
1.0
|
O3G
|
A:ATP600
|
3.6
|
5.3
|
1.0
|
O3B
|
A:ATP600
|
3.7
|
5.3
|
1.0
|
CG2
|
A:THR179
|
4.0
|
12.9
|
1.0
|
O2B
|
A:ATP600
|
4.1
|
5.3
|
1.0
|
OD1
|
A:ASP272
|
4.1
|
10.0
|
1.0
|
N
|
A:THR179
|
4.3
|
12.9
|
1.0
|
CA
|
A:THR179
|
4.4
|
12.9
|
1.0
|
O1A
|
A:ATP600
|
4.4
|
5.3
|
1.0
|
O3A
|
A:ATP600
|
4.5
|
5.3
|
1.0
|
OD2
|
A:ASP272
|
4.5
|
10.0
|
1.0
|
O2G
|
A:ATP600
|
4.7
|
5.3
|
1.0
|
CG
|
A:ASP272
|
4.7
|
10.0
|
1.0
|
PA
|
A:ATP600
|
4.8
|
5.3
|
1.0
|
|
Magnesium binding site 2 out
of 5 in 8j0s
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Magnesium Binding Sites List in 8j0s
Magnesium binding site 2 out
of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg601
b:20.0
occ:1.00
|
O3G
|
B:ATP600
|
2.0
|
15.4
|
1.0
|
OG1
|
B:THR179
|
2.0
|
17.9
|
1.0
|
O2B
|
B:ATP600
|
2.3
|
15.4
|
1.0
|
CB
|
B:THR179
|
3.3
|
17.9
|
1.0
|
PG
|
B:ATP600
|
3.4
|
15.4
|
1.0
|
PB
|
B:ATP600
|
3.5
|
15.4
|
1.0
|
OD1
|
B:ASP272
|
3.5
|
13.5
|
1.0
|
O3B
|
B:ATP600
|
3.7
|
15.4
|
1.0
|
OE1
|
B:GLN211
|
3.8
|
13.1
|
1.0
|
CG2
|
B:THR179
|
4.0
|
17.9
|
1.0
|
OD2
|
B:ASP272
|
4.1
|
13.5
|
1.0
|
CG
|
B:ASP272
|
4.2
|
13.5
|
1.0
|
O1G
|
B:ATP600
|
4.3
|
15.4
|
1.0
|
N
|
B:THR179
|
4.3
|
17.9
|
1.0
|
O2G
|
B:ATP600
|
4.3
|
15.4
|
1.0
|
O1B
|
B:ATP600
|
4.4
|
15.4
|
1.0
|
CA
|
B:THR179
|
4.4
|
17.9
|
1.0
|
O1A
|
B:ATP600
|
4.4
|
15.4
|
1.0
|
O3A
|
B:ATP600
|
4.7
|
15.4
|
1.0
|
CD
|
B:GLN211
|
4.7
|
13.1
|
1.0
|
PA
|
B:ATP600
|
4.9
|
15.4
|
1.0
|
|
Magnesium binding site 3 out
of 5 in 8j0s
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Magnesium Binding Sites List in 8j0s
Magnesium binding site 3 out
of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg601
b:11.3
occ:1.00
|
O2B
|
C:ATP600
|
1.9
|
0.0
|
1.0
|
OG1
|
C:THR179
|
2.0
|
12.0
|
1.0
|
O1G
|
C:ATP600
|
2.3
|
0.0
|
1.0
|
CB
|
C:THR179
|
3.2
|
12.0
|
1.0
|
PB
|
C:ATP600
|
3.2
|
0.0
|
1.0
|
PG
|
C:ATP600
|
3.3
|
0.0
|
1.0
|
O2G
|
C:ATP600
|
3.6
|
0.0
|
1.0
|
O3B
|
C:ATP600
|
3.7
|
0.0
|
1.0
|
CG2
|
C:THR179
|
4.0
|
12.0
|
1.0
|
O1B
|
C:ATP600
|
4.0
|
0.0
|
1.0
|
OD1
|
C:ASP272
|
4.0
|
12.4
|
1.0
|
N
|
C:THR179
|
4.2
|
12.0
|
1.0
|
CA
|
C:THR179
|
4.3
|
12.0
|
1.0
|
O1A
|
C:ATP600
|
4.3
|
0.0
|
1.0
|
OD2
|
C:ASP272
|
4.4
|
12.4
|
1.0
|
O3A
|
C:ATP600
|
4.4
|
0.0
|
1.0
|
CG
|
C:ASP272
|
4.6
|
12.4
|
1.0
|
O3G
|
C:ATP600
|
4.7
|
0.0
|
1.0
|
PA
|
C:ATP600
|
4.7
|
0.0
|
1.0
|
O2A
|
C:ATP600
|
4.8
|
0.0
|
1.0
|
|
Magnesium binding site 4 out
of 5 in 8j0s
Go back to
Magnesium Binding Sites List in 8j0s
Magnesium binding site 4 out
of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg601
b:15.4
occ:1.00
|
O1B
|
D:ADP600
|
1.8
|
8.0
|
1.0
|
OG1
|
D:THR178
|
2.0
|
15.9
|
1.0
|
PB
|
D:ADP600
|
3.1
|
8.0
|
1.0
|
CB
|
D:THR178
|
3.4
|
15.9
|
1.0
|
OE1
|
D:GLU203
|
3.4
|
16.4
|
1.0
|
O2B
|
D:ADP600
|
3.5
|
8.0
|
1.0
|
NH1
|
D:ARG204
|
3.7
|
14.6
|
1.0
|
N
|
D:THR178
|
3.9
|
15.9
|
1.0
|
CA
|
D:THR178
|
4.1
|
15.9
|
1.0
|
O3A
|
D:ADP600
|
4.1
|
8.0
|
1.0
|
CD
|
D:GLU203
|
4.2
|
16.4
|
1.0
|
O3B
|
D:ADP600
|
4.2
|
8.0
|
1.0
|
OD1
|
D:ASP265
|
4.2
|
13.3
|
1.0
|
OE1
|
D:GLU207
|
4.2
|
17.7
|
1.0
|
CG2
|
D:THR178
|
4.4
|
15.9
|
1.0
|
OD2
|
D:ASP265
|
4.5
|
13.3
|
1.0
|
ND2
|
D:ASN266
|
4.5
|
12.8
|
1.0
|
CE
|
D:LYS177
|
4.5
|
13.3
|
1.0
|
CB
|
D:LYS177
|
4.5
|
13.3
|
1.0
|
O1A
|
D:ADP600
|
4.5
|
8.0
|
1.0
|
OE2
|
D:GLU203
|
4.6
|
16.4
|
1.0
|
OE2
|
D:GLU207
|
4.6
|
17.7
|
1.0
|
CG
|
D:ASP265
|
4.7
|
13.3
|
1.0
|
C
|
D:LYS177
|
4.8
|
13.3
|
1.0
|
CD
|
D:GLU207
|
4.9
|
17.7
|
1.0
|
PA
|
D:ADP600
|
4.9
|
8.0
|
1.0
|
NZ
|
D:LYS177
|
4.9
|
13.3
|
1.0
|
CZ
|
D:ARG204
|
4.9
|
14.6
|
1.0
|
|
Magnesium binding site 5 out
of 5 in 8j0s
Go back to
Magnesium Binding Sites List in 8j0s
Magnesium binding site 5 out
of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq)
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in Complex with Bedaquiline(Bdq) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg601
b:11.7
occ:1.00
|
OG1
|
F:THR178
|
2.0
|
10.2
|
1.0
|
O1B
|
F:ADP600
|
2.7
|
5.3
|
1.0
|
O1A
|
F:ADP600
|
2.8
|
5.3
|
1.0
|
CB
|
F:THR178
|
3.3
|
10.2
|
1.0
|
OE1
|
F:GLU203
|
3.4
|
11.6
|
1.0
|
NH1
|
F:ARG204
|
3.6
|
11.8
|
1.0
|
PB
|
F:ADP600
|
3.8
|
5.3
|
1.0
|
PA
|
F:ADP600
|
3.9
|
5.3
|
1.0
|
OE2
|
F:GLU207
|
4.0
|
13.4
|
1.0
|
O3A
|
F:ADP600
|
4.1
|
5.3
|
1.0
|
OE1
|
F:GLU207
|
4.1
|
13.4
|
1.0
|
O2B
|
F:ADP600
|
4.1
|
5.3
|
1.0
|
CG2
|
F:THR178
|
4.2
|
10.2
|
1.0
|
N
|
F:THR178
|
4.2
|
10.2
|
1.0
|
CA
|
F:THR178
|
4.3
|
10.2
|
1.0
|
CD
|
F:GLU203
|
4.3
|
11.6
|
1.0
|
CD
|
F:GLU207
|
4.5
|
13.4
|
1.0
|
O2A
|
F:ADP600
|
4.5
|
5.3
|
1.0
|
OD1
|
F:ASP265
|
4.6
|
10.9
|
1.0
|
OD2
|
F:ASP265
|
4.7
|
10.9
|
1.0
|
OE2
|
F:GLU203
|
4.9
|
11.6
|
1.0
|
CZ
|
F:ARG204
|
4.9
|
11.8
|
1.0
|
ND2
|
F:ASN266
|
4.9
|
10.0
|
1.0
|
|
Reference:
Y.Zhang,
Y.Lai,
F.Liu,
Z.Rao,
H.Gong.
Structure of Mycobacterium Tuberculosis Atp Synthase To Be Published.
Page generated: Fri Oct 4 11:27:41 2024
|