Atomistry » Magnesium » PDB 7fsa-7jhn » 7jga
Atomistry »
  Magnesium »
    PDB 7fsa-7jhn »
      7jga »

Magnesium in PDB 7jga: Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3

Enzymatic activity of Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3

All present enzymatic activity of Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3:
7.1.2.2;

Other elements in 7jga:

The structure of Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3 also contains other interesting chemical elements:

Bromine (Br) 7 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3 (pdb code 7jga). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3, PDB code: 7jga:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 7jga

Go back to Magnesium Binding Sites List in 7jga
Magnesium binding site 1 out of 4 in the Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3


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 Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:75.4
occ:1.00
O1B A:ATP600 1.8 78.3 1.0
O1G A:ATP600 2.0 78.3 1.0
OG1 A:THR179 2.0 75.9 1.0
PG A:ATP600 2.9 78.3 1.0
PB A:ATP600 2.9 78.3 1.0
O3G A:ATP600 3.0 78.3 1.0
CB A:THR179 3.2 75.9 1.0
O3B A:ATP600 3.4 78.3 1.0
O2B A:ATP600 3.7 78.3 1.0
NE2 A:GLN211 3.8 74.4 1.0
CG2 A:THR179 3.9 75.9 1.0
O1A A:ATP600 4.0 78.3 1.0
OD2 A:ASP272 4.0 74.1 1.0
OD1 A:ASP272 4.2 74.1 1.0
O3A A:ATP600 4.2 78.3 1.0
O2G A:ATP600 4.3 78.3 1.0
CA A:THR179 4.3 75.9 1.0
N A:THR179 4.4 75.9 1.0
CG A:ASP272 4.5 74.1 1.0
PA A:ATP600 4.6 78.3 1.0
CD A:GLN211 4.8 74.4 1.0
OE1 A:GLN211 4.8 74.4 1.0

Magnesium binding site 2 out of 4 in 7jga

Go back to Magnesium Binding Sites List in 7jga
Magnesium binding site 2 out of 4 in the Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3


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 Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:75.1
occ:1.00
O2B B:ATP600 2.0 82.2 1.0
O3G B:ATP600 2.0 82.2 1.0
OG1 B:THR179 2.1 75.3 1.0
OD2 B:ASP272 3.1 71.7 1.0
CB B:THR179 3.2 75.3 1.0
PB B:ATP600 3.2 82.2 1.0
PG B:ATP600 3.3 82.2 1.0
NE2 B:GLN211 3.4 73.7 1.0
O1B B:ATP600 3.7 82.2 1.0
O3B B:ATP600 3.8 82.2 1.0
OD1 B:ASP272 3.8 71.7 1.0
CG B:ASP272 3.9 71.7 1.0
O2G B:ATP600 3.9 82.2 1.0
CG2 B:THR179 4.0 75.3 1.0
CD B:GLN211 4.1 73.7 1.0
O1A B:ATP600 4.1 82.2 1.0
N B:THR179 4.3 75.3 1.0
CA B:THR179 4.3 75.3 1.0
O3A B:ATP600 4.5 82.2 1.0
O1G B:ATP600 4.5 82.2 1.0
OE1 B:GLN211 4.6 73.7 1.0
PA B:ATP600 4.8 82.2 1.0
CG2 B:THR215 4.8 74.1 1.0
CG B:GLN211 4.9 73.7 1.0

Magnesium binding site 3 out of 4 in 7jga

Go back to Magnesium Binding Sites List in 7jga
Magnesium binding site 3 out of 4 in the Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3


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 Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:79.5
occ:1.00
O2B C:ATP600 1.8 76.4 1.0
O1B C:ATP600 2.1 76.4 1.0
OG1 C:THR179 2.1 73.3 1.0
O1G C:ATP600 2.1 76.4 1.0
PB C:ATP600 2.1 76.4 1.0
O3B C:ATP600 3.0 76.4 1.0
PG C:ATP600 3.1 76.4 1.0
CB C:THR179 3.4 73.3 1.0
O3A C:ATP600 3.6 76.4 1.0
O2G C:ATP600 3.8 76.4 1.0
O1A C:ATP600 3.9 76.4 1.0
OD2 C:ASP272 4.0 72.1 1.0
OD1 C:ASP272 4.1 72.1 1.0
N C:THR179 4.2 73.3 1.0
CG2 C:THR179 4.2 73.3 1.0
PA C:ATP600 4.3 76.4 1.0
NE2 C:GLN211 4.3 72.4 1.0
O3G C:ATP600 4.3 76.4 1.0
CA C:THR179 4.4 73.3 1.0
CG C:ASP272 4.5 72.1 1.0
NZ C:LYS178 4.6 73.9 1.0
O2A C:ATP600 4.6 76.4 1.0
CE C:LYS178 4.8 73.9 1.0
OD1 C:ASP273 4.9 73.5 1.0
OD2 C:ASP273 4.9 73.5 1.0

Magnesium binding site 4 out of 4 in 7jga

Go back to Magnesium Binding Sites List in 7jga
Magnesium binding site 4 out of 4 in the Cryo-Em Structure of Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3


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 Bedaquiline-Saturated Mycobacterium Smegmatis Atp Synthase Rotational State 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg601

b:75.4
occ:1.00
OG1 E:THR167 2.1 76.8 1.0
OE2 E:GLU192 2.1 76.0 1.0
O2B E:ADP600 2.2 77.4 1.0
O3B E:ADP600 2.5 77.4 1.0
PB E:ADP600 2.8 77.4 1.0
CD E:GLU192 3.2 76.0 1.0
CB E:THR167 3.4 76.8 1.0
O3A E:ADP600 3.9 77.4 1.0
NH1 E:ARG193 3.9 74.5 1.0
N E:THR167 4.0 76.8 1.0
OE1 E:GLU192 4.0 76.0 1.0
CG E:GLU192 4.1 76.0 1.0
O1B E:ADP600 4.1 77.4 1.0
CA E:THR167 4.3 76.8 1.0
O2A E:ADP600 4.3 77.4 1.0
NZ E:LYS166 4.3 75.2 1.0
CE E:LYS166 4.3 75.2 1.0
CG2 E:THR167 4.4 76.8 1.0
PA E:ADP600 4.5 77.4 1.0
CB E:LYS166 4.7 75.2 1.0
O1A E:ADP600 4.8 77.4 1.0
CZ E:ARG193 4.8 74.5 1.0
C E:LYS166 5.0 75.2 1.0

Reference:

H.Guo, G.M.Courbon, S.A.Bueler, J.Mai, J.Liu, J.L.Rubinstein. Structure of Mycobacterial Atp Synthase with the Tb Drug Bedaquiline Biorxiv 2020.
DOI: 10.1101/2020.08.06.225375
Page generated: Wed Oct 2 21:51:21 2024

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy