Magnesium in PDB 7nkh: Mycobacterium Smegmatis Atp Synthase F1 State 2

All present enzymatic activity of Mycobacterium Smegmatis Atp Synthase F1 State 2:
7.1.2.2;

The binding sites of Magnesium atom in the Mycobacterium Smegmatis Atp Synthase F1 State 2 (pdb code 7nkh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Mycobacterium Smegmatis Atp Synthase F1 State 2, PDB code: 7nkh:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Mycobacterium Smegmatis Atp Synthase F1 State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mycobacterium Smegmatis Atp Synthase F1 State 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:50.7 occ:1.00 O2G A:ATP600 2.2 54.2 1.0 O A:HOH703 2.2 51.4 1.0 OG1 A:THR179 2.2 50.7 1.0 O A:HOH701 2.2 53.2 1.0 O2B A:ATP600 2.2 54.2 1.0 O A:HOH702 2.2 53.7 1.0 HB A:THR179 3.0 50.7 1.0 CB A:THR179 3.2 50.7 1.0 O3B A:ATP600 3.2 54.2 1.0 PG A:ATP600 3.2 54.2 1.0 PB A:ATP600 3.3 54.2 1.0 H A:THR179 3.3 50.7 1.0 O3G A:ATP600 3.7 54.2 1.0 OD2 A:ASP272 3.8 50.6 1.0 N A:THR179 4.0 50.7 1.0 HG21 A:THR179 4.0 50.7 1.0 OD1 A:ASP272 4.0 50.6 1.0 CA A:THR179 4.2 50.7 1.0 O3A A:ATP600 4.2 54.2 1.0 CG2 A:THR179 4.2 50.7 1.0 O2A A:ATP600 4.3 54.2 1.0 HB2 A:LYS178 4.3 51.3 1.0 O1B A:ATP600 4.4 54.2 1.0 CG A:ASP272 4.4 50.6 1.0 HA A:THR179 4.5 50.7 1.0 HE2 A:LYS178 4.5 51.3 1.0 O1G A:ATP600 4.5 54.2 1.0 PA A:ATP600 4.7 54.2 1.0 HZ3 A:LYS178 4.7 51.3 1.0 HG23 A:THR179 4.8 50.7 1.0 HD13 A:ILE329 4.8 49.6 1.0 HZ1 A:LYS178 4.8 51.3 1.0 O1A A:ATP600 4.9 54.2 1.0 HG22 A:THR179 4.9 50.7 1.0 HG21 A:ILE329 4.9 49.6 1.0

Magnesium binding site 2 out of 5 in the Mycobacterium Smegmatis Atp Synthase F1 State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mycobacterium Smegmatis Atp Synthase F1 State 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:55.1 occ:1.00 OG1 B:THR179 2.2 52.0 1.0 O B:HOH701 2.2 54.3 1.0 O B:HOH702 2.2 55.2 1.0 O2G B:ATP600 2.2 58.3 1.0 O2B B:ATP600 2.2 58.3 1.0 O B:HOH703 2.2 51.2 1.0 HB B:THR179 2.8 52.0 1.0 CB B:THR179 3.0 52.0 1.0 PB B:ATP600 3.4 58.3 1.0 O3B B:ATP600 3.4 58.3 1.0 PG B:ATP600 3.4 58.3 1.0 H B:THR179 3.4 52.0 1.0 OD2 B:ASP272 3.8 50.0 1.0 HG21 B:THR179 3.8 52.0 1.0 OD1 B:ASP272 3.9 50.0 1.0 OE1 B:GLN211 4.0 51.3 1.0 CG2 B:THR179 4.0 52.0 1.0 N B:THR179 4.1 52.0 1.0 CA B:THR179 4.1 52.0 1.0 CG B:ASP272 4.3 50.0 1.0 O3G B:ATP600 4.3 58.3 1.0 O3A B:ATP600 4.4 58.3 1.0 O1A B:ATP600 4.4 58.3 1.0 O1B B:ATP600 4.4 58.3 1.0 HB2 B:LYS178 4.4 53.0 1.0 O1G B:ATP600 4.5 58.3 1.0 HA B:THR179 4.5 52.0 1.0 HE2 B:LYS178 4.5 53.0 1.0 HG22 B:THR179 4.6 52.0 1.0 HG23 B:THR179 4.7 52.0 1.0 PA B:ATP600 4.8 58.3 1.0 HH B:TYR206 4.9 47.5 1.0 O2A B:ATP600 5.0 58.3 1.0

Magnesium binding site 3 out of 5 in the Mycobacterium Smegmatis Atp Synthase F1 State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Mycobacterium Smegmatis Atp Synthase F1 State 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:53.6 occ:1.00 OG1 C:THR179 2.2 50.1 1.0 O2G C:ATP600 2.2 52.1 1.0 O2B C:ATP600 2.2 52.1 1.0 O C:HOH703 2.2 50.6 1.0 O C:HOH702 2.2 48.3 1.0 O C:HOH701 2.2 51.2 1.0 HB C:THR179 2.9 50.1 1.0 CB C:THR179 3.1 50.1 1.0 PB C:ATP600 3.4 52.1 1.0 H C:THR179 3.4 50.1 1.0 O3B C:ATP600 3.4 52.1 1.0 PG C:ATP600 3.4 52.1 1.0 OD2 C:ASP272 3.8 48.5 1.0 HG21 C:THR179 3.9 50.1 1.0 N C:THR179 4.0 50.1 1.0 OD1 C:ASP272 4.1 48.5 1.0 CG2 C:THR179 4.1 50.1 1.0 O1A C:ATP600 4.1 52.1 1.0 CA C:THR179 4.1 50.1 1.0 O3G C:ATP600 4.3 52.1 1.0 O3A C:ATP600 4.3 52.1 1.0 CG C:ASP272 4.4 48.5 1.0 HB2 C:LYS178 4.4 49.8 1.0 HE2 C:LYS178 4.4 49.8 1.0 O1B C:ATP600 4.4 52.1 1.0 O1G C:ATP600 4.5 52.1 1.0 HA C:THR179 4.5 50.1 1.0 PA C:ATP600 4.6 52.1 1.0 HG22 C:THR179 4.7 50.1 1.0 HG23 C:THR179 4.7 50.1 1.0 HG21 C:ILE329 4.9 48.3 1.0 O2A C:ATP600 4.9 52.1 1.0

Magnesium binding site 4 out of 5 in the Mycobacterium Smegmatis Atp Synthase F1 State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Mycobacterium Smegmatis Atp Synthase F1 State 2 within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg601 b:51.4 occ:1.00 O D:HOH701 2.2 54.1 1.0 O2B D:ADP600 2.2 53.9 1.0 O D:HOH702 2.2 54.4 1.0 O D:HOH704 2.2 55.3 1.0 O D:HOH703 2.2 54.3 1.0 OG1 D:THR167 2.2 53.0 1.0 HB D:THR167 3.1 53.0 1.0 HH12 D:ARG193 3.1 52.8 1.0 CB D:THR167 3.2 53.0 1.0 PB D:ADP600 3.3 53.9 1.0 H D:THR167 3.5 53.0 1.0 O3B D:ADP600 3.6 53.9 1.0 O3A D:ADP600 3.6 53.9 1.0 OE2 D:GLU196 3.7 54.9 1.0 NH1 D:ARG193 3.7 52.8 1.0 HH12 C:ARG376 3.8 52.4 1.0 HH11 D:ARG193 3.8 52.8 1.0 HH11 C:ARG376 3.8 52.4 1.0 OE1 D:GLU196 3.9 54.9 1.0 N D:THR167 4.0 53.0 1.0 OE1 D:GLU192 4.1 54.8 1.0 HG21 D:THR167 4.1 53.0 1.0 NH1 C:ARG376 4.1 52.4 1.0 HB2 D:LYS166 4.1 51.3 1.0 CA D:THR167 4.2 53.0 1.0 O2A D:ADP600 4.2 53.9 1.0 OD2 D:ASP254 4.2 52.2 1.0 CD D:GLU196 4.2 54.9 1.0 CG2 D:THR167 4.3 53.0 1.0 PA D:ADP600 4.3 53.9 1.0 HA D:THR167 4.4 53.0 1.0 CD D:GLU192 4.4 54.8 1.0 HE2 D:LYS166 4.4 51.3 1.0 OD1 D:ASP254 4.5 52.2 1.0 O1A D:ADP600 4.5 53.9 1.0 O1B D:ADP600 4.6 53.9 1.0 OE2 D:GLU192 4.6 54.8 1.0 HH22 D:ARG193 4.7 52.8 1.0 CZ D:ARG193 4.8 52.8 1.0 HG3 D:GLU192 4.8 54.8 1.0 CG D:ASP254 4.8 52.2 1.0 HG23 D:THR167 4.8 53.0 1.0 HG22 D:THR167 4.9 53.0 1.0

Magnesium binding site 5 out of 5 in the Mycobacterium Smegmatis Atp Synthase F1 State 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Mycobacterium Smegmatis Atp Synthase F1 State 2 within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:47.1 occ:1.00 O2G F:ATP600 2.2 52.5 1.0 OG1 F:THR167 2.2 49.4 1.0 O F:HOH701 2.2 50.1 1.0 O2B F:ATP600 2.2 52.5 1.0 O F:HOH703 2.2 47.1 1.0 O F:HOH702 2.2 51.2 1.0 HB F:THR167 3.0 49.4 1.0 HH12 F:ARG193 3.1 49.6 1.0 CB F:THR167 3.2 49.4 1.0 OE1 F:GLU192 3.3 49.7 1.0 H F:THR167 3.4 49.4 1.0 PB F:ATP600 3.4 52.5 1.0 O3B F:ATP600 3.4 52.5 1.0 PG F:ATP600 3.4 52.5 1.0 HH11 F:ARG193 3.6 49.6 1.0 OE2 F:GLU196 3.6 51.6 1.0 NH1 F:ARG193 3.7 49.6 1.0 HH12 B:ARG376 3.8 52.7 1.0 OE1 F:GLU196 3.9 51.6 1.0 O2A F:ATP600 3.9 52.5 1.0 N F:THR167 3.9 49.4 1.0 HB2 F:LYS166 4.0 48.3 1.0 HG21 F:THR167 4.1 49.4 1.0 CA F:THR167 4.1 49.4 1.0 CD F:GLU196 4.2 51.6 1.0 CG2 F:THR167 4.2 49.4 1.0 O3A F:ATP600 4.2 52.5 1.0 HE2 F:LYS166 4.3 48.3 1.0 O3G F:ATP600 4.4 52.5 1.0 O1G F:ATP600 4.4 52.5 1.0 HA F:THR167 4.4 49.4 1.0 HH11 B:ARG376 4.4 52.7 1.0 NH1 B:ARG376 4.5 52.7 1.0 CD F:GLU192 4.5 49.7 1.0 O1B F:ATP600 4.5 52.5 1.0 PA F:ATP600 4.6 52.5 1.0 OD2 F:ASP254 4.6 49.2 1.0 OD1 F:ASP254 4.7 49.2 1.0 HG23 F:THR167 4.8 49.4 1.0 O1A F:ATP600 4.8 52.5 1.0 HZ3 F:LYS166 4.8 48.3 1.0 HZ1 F:LYS166 4.9 48.3 1.0 HG22 F:THR167 4.9 49.4 1.0 CB F:LYS166 4.9 48.3 1.0 CZ F:ARG193 4.9 49.6 1.0 HB3 F:LYS166 5.0 48.3 1.0

J.Petri, M.G.Montgomery, T.J.Spikes, G.M.Cook, J.E.Walker. Structure of the Atp Synthase From Mycobacterium Smegmatis To Be Published.