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Magnesium in PDB 8j0t: Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form

Enzymatic activity of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form

All present enzymatic activity of Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form:
7.1.2.2;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form (pdb code 8j0t). 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 the Apo-Form, PDB code: 8j0t:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 8j0t

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Magnesium binding site 1 out of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form


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 the Apo-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:43.0
occ:1.00
OG1 A:THR179 2.0 45.4 1.0
O1B A:ATP600 2.0 23.4 1.0
O1G A:ATP600 2.5 23.4 1.0
CB A:THR179 3.2 45.4 1.0
PB A:ATP600 3.4 23.4 1.0
PG A:ATP600 3.5 23.4 1.0
O3G A:ATP600 3.6 23.4 1.0
O3B A:ATP600 3.9 23.4 1.0
CG2 A:THR179 3.9 45.4 1.0
O2B A:ATP600 4.1 23.4 1.0
OD1 A:ASP272 4.2 42.6 1.0
O2A A:ATP600 4.2 23.4 1.0
CA A:THR179 4.4 45.4 1.0
N A:THR179 4.4 45.4 1.0
O3A A:ATP600 4.6 23.4 1.0
OD2 A:ASP272 4.7 42.6 1.0
PA A:ATP600 4.8 23.4 1.0
CG A:ASP272 4.8 42.6 1.0
O2G A:ATP600 4.9 23.4 1.0
OD2 A:ASP273 4.9 44.1 1.0

Magnesium binding site 2 out of 5 in 8j0t

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Magnesium binding site 2 out of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form


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 the Apo-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:59.3
occ:1.00
OG1 B:THR179 2.0 54.6 1.0
O1B B:ATP600 2.1 32.0 1.0
CB B:THR179 2.9 54.6 1.0
O1G B:ATP600 3.0 32.0 1.0
O3G B:ATP600 3.4 32.0 1.0
CG2 B:THR179 3.4 54.6 1.0
PB B:ATP600 3.5 32.0 1.0
PG B:ATP600 3.6 32.0 1.0
O2A B:ATP600 3.6 32.0 1.0
OE1 B:GLN211 3.8 48.1 1.0
O3B B:ATP600 4.0 32.0 1.0
CG2 B:THR215 4.2 49.9 1.0
CA B:THR179 4.3 54.6 1.0
PA B:ATP600 4.4 32.0 1.0
OD1 B:ASP272 4.5 45.4 1.0
O3A B:ATP600 4.5 32.0 1.0
N B:THR179 4.5 54.6 1.0
O2B B:ATP600 4.6 32.0 1.0
O1A B:ATP600 4.8 32.0 1.0
OD2 B:ASP272 4.8 45.4 1.0
CD B:GLN211 5.0 48.1 1.0

Magnesium binding site 3 out of 5 in 8j0t

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Magnesium binding site 3 out of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form


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 the Apo-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:54.7
occ:1.00
O1B C:ATP600 1.9 25.9 1.0
OG1 C:THR179 2.0 48.4 1.0
O1G C:ATP600 2.4 25.9 1.0
CB C:THR179 3.2 48.4 1.0
PB C:ATP600 3.2 25.9 1.0
PG C:ATP600 3.4 25.9 1.0
O3G C:ATP600 3.6 25.9 1.0
O3B C:ATP600 3.8 25.9 1.0
CG2 C:THR179 3.9 48.4 1.0
O2B C:ATP600 4.0 25.9 1.0
OD1 C:ASP272 4.2 43.8 1.0
O2A C:ATP600 4.2 25.9 1.0
N C:THR179 4.3 48.4 1.0
CA C:THR179 4.3 48.4 1.0
O3A C:ATP600 4.4 25.9 1.0
PA C:ATP600 4.7 25.9 1.0
OD2 C:ASP272 4.7 43.8 1.0
O2G C:ATP600 4.7 25.9 1.0
CG C:ASP272 4.8 43.8 1.0
O1A C:ATP600 4.9 25.9 1.0

Magnesium binding site 4 out of 5 in 8j0t

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Magnesium binding site 4 out of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form


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 the Apo-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg601

b:49.3
occ:1.00
OG1 D:THR178 2.0 50.0 1.0
O3B D:ADP600 2.1 18.3 1.0
CB D:THR178 3.3 50.0 1.0
PB D:ADP600 3.4 18.3 1.0
OE1 D:GLU203 3.7 49.8 1.0
ND2 D:ASN266 3.9 44.8 1.0
N D:THR178 3.9 50.0 1.0
NH1 D:ARG204 3.9 46.9 1.0
O2B D:ADP600 4.0 18.3 1.0
CA D:THR178 4.1 50.0 1.0
O1B D:ADP600 4.1 18.3 1.0
OE1 D:GLU207 4.2 51.1 1.0
OD1 D:ASP265 4.2 46.0 1.0
CD D:GLU203 4.3 49.8 1.0
CG2 D:THR178 4.3 50.0 1.0
OD2 D:ASP265 4.4 46.0 1.0
OE2 D:GLU207 4.4 51.1 1.0
O3A D:ADP600 4.5 18.3 1.0
O2A D:ADP600 4.6 18.3 1.0
CG D:ASP265 4.7 46.0 1.0
CB D:LYS177 4.7 45.6 1.0
OE2 D:GLU203 4.7 49.8 1.0
CD D:GLU207 4.7 51.1 1.0
NH1 C:ARG376 4.7 45.7 1.0
CE D:LYS177 4.8 45.6 1.0
C D:LYS177 4.9 45.6 1.0
CG D:GLU203 4.9 49.8 1.0
PA D:ADP600 4.9 18.3 1.0
CG D:ASN266 5.0 44.8 1.0

Magnesium binding site 5 out of 5 in 8j0t

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Magnesium binding site 5 out of 5 in the Cryo-Em Structure of Mycobacterium Tuberculosis Atp Synthase in the Apo-Form


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 the Apo-Form within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg601

b:47.9
occ:1.00
OG1 F:THR178 2.0 47.4 1.0
O3B F:ADP600 2.1 20.6 1.0
PB F:ADP600 3.3 20.6 1.0
CB F:THR178 3.4 47.4 1.0
OE1 F:GLU203 3.7 48.7 1.0
O2B F:ADP600 3.8 20.6 1.0
O1B F:ADP600 3.9 20.6 1.0
N F:THR178 4.0 47.4 1.0
OD1 F:ASP265 4.1 42.8 1.0
NH1 F:ARG204 4.2 48.1 1.0
OE2 F:GLU207 4.2 51.4 1.0
CD F:GLU203 4.2 48.7 1.0
CA F:THR178 4.2 47.4 1.0
CG2 F:THR178 4.3 47.4 1.0
OE1 F:GLU207 4.4 51.4 1.0
OD2 F:ASP265 4.4 42.8 1.0
ND2 F:ASN266 4.5 43.1 1.0
CE F:LYS177 4.5 42.7 1.0
O3A F:ADP600 4.5 20.6 1.0
CG F:ASP265 4.6 42.8 1.0
CB F:LYS177 4.6 42.7 1.0
CD F:GLU207 4.7 51.4 1.0
OE2 F:GLU203 4.7 48.7 1.0
O2A F:ADP600 4.8 20.6 1.0
CG F:GLU203 4.8 48.7 1.0
C F:LYS177 4.9 42.7 1.0
NZ F:LYS177 4.9 42.7 1.0
PA F:ADP600 5.0 20.6 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 11:27:43 2024

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