Magnesium in PDB 8ki3: Structure of the Human Atp Synthase Bound to Bedaquiline (Composite)

The structure of Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) also contains other interesting chemical elements:

Bromine

(Br)

1 atom

The binding sites of Magnesium atom in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) (pdb code 8ki3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite), PDB code: 8ki3:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:66.1 occ:1.00 O3G A:ATP601 1.9 73.7 1.0 O1B A:ATP601 1.9 73.7 1.0 OG1 A:THR176 2.0 62.5 1.0 PB A:ATP601 3.1 73.7 1.0 PG A:ATP601 3.2 73.7 1.0 CB A:THR176 3.2 62.5 1.0 O3B A:ATP601 3.6 73.7 1.0 O2B A:ATP601 3.7 73.7 1.0 O1G A:ATP601 3.8 73.7 1.0 CG2 A:THR176 4.1 62.5 1.0 OD2 A:ASP269 4.1 56.4 1.0 OD1 A:ASP269 4.1 56.4 1.0 N A:THR176 4.2 62.5 1.0 CA A:THR176 4.3 62.5 1.0 O2G A:ATP601 4.3 73.7 1.0 O3A A:ATP601 4.5 73.7 1.0 O2A A:ATP601 4.5 73.7 1.0 CG A:ASP269 4.5 56.4 1.0 PA A:ATP601 4.9 73.7 1.0

Magnesium binding site 2 out of 5 in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:63.3 occ:1.00 OG1 B:THR176 2.1 61.7 1.0 O1B B:ATP601 2.2 71.3 1.0 O3G B:ATP601 2.5 71.3 1.0 CB B:THR176 3.4 61.7 1.0 OD1 B:ASP269 3.5 51.2 1.0 PB B:ATP601 3.5 71.3 1.0 PG B:ATP601 3.6 71.3 1.0 OD2 B:ASP269 3.8 51.2 1.0 O2G B:ATP601 4.0 71.3 1.0 OE1 B:GLN208 4.0 54.6 1.0 O3B B:ATP601 4.0 71.3 1.0 CG B:ASP269 4.0 51.2 1.0 O2B B:ATP601 4.1 71.3 1.0 N B:THR176 4.2 61.7 1.0 CG2 B:THR176 4.3 61.7 1.0 CA B:THR176 4.4 61.7 1.0 O1A B:ATP601 4.6 71.3 1.0 CD B:GLN208 4.6 54.6 1.0 O3A B:ATP601 4.8 71.3 1.0 O1G B:ATP601 4.9 71.3 1.0 NE2 B:GLN208 4.9 54.6 1.0

Magnesium binding site 3 out of 5 in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg602 b:70.2 occ:1.00 O1B C:ATP601 2.0 72.4 1.0 OG1 C:THR176 2.0 65.1 1.0 O1G C:ATP601 2.1 72.4 1.0 CB C:THR176 3.3 65.1 1.0 PB C:ATP601 3.3 72.4 1.0 PG C:ATP601 3.3 72.4 1.0 O3B C:ATP601 3.7 72.4 1.0 O2A C:ATP601 3.8 72.4 1.0 O3G C:ATP601 3.9 72.4 1.0 CG2 C:THR176 4.0 65.1 1.0 OD2 C:ASP269 4.0 53.1 1.0 O2B C:ATP601 4.1 72.4 1.0 OD1 C:ASP269 4.1 53.1 1.0 N C:THR176 4.3 65.1 1.0 CA C:THR176 4.4 65.1 1.0 O3A C:ATP601 4.5 72.4 1.0 CG C:ASP269 4.5 53.1 1.0 O2G C:ATP601 4.6 72.4 1.0 OE1 C:GLN208 4.6 55.3 1.0 PA C:ATP601 4.7 72.4 1.0

Magnesium binding site 4 out of 5 in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg502 b:74.4 occ:1.00 OG1 D:THR166 2.1 81.4 1.0 O1B D:ADP501 2.2 89.6 1.0 CB D:THR166 3.4 81.4 1.0 OE1 D:GLU191 3.5 65.5 1.0 PB D:ADP501 3.7 89.6 1.0 OD1 D:ASP259 3.9 63.3 1.0 OD2 D:ASP259 3.9 63.3 1.0 N D:THR166 3.9 81.4 1.0 CD D:GLU191 4.0 65.5 1.0 CA D:THR166 4.1 81.4 1.0 OE2 D:GLU195 4.1 70.7 1.0 O2B D:ADP501 4.1 89.6 1.0 NH1 D:ARG192 4.2 65.1 1.0 O1A D:ADP501 4.2 89.6 1.0 CG D:ASP259 4.3 63.3 1.0 O3B D:ADP501 4.4 89.6 1.0 CG2 D:THR166 4.4 81.4 1.0 OE2 D:GLU191 4.4 65.5 1.0 CB D:LYS165 4.6 79.2 1.0 OE1 D:GLU195 4.6 70.7 1.0 CE D:LYS165 4.6 79.2 1.0 O3A D:ADP501 4.7 89.6 1.0 CG D:GLU191 4.7 65.5 1.0 C D:LYS165 4.8 79.2 1.0 CD D:GLU195 4.8 70.7 1.0 NZ D:LYS165 4.9 79.2 1.0 PA D:ADP501 4.9 89.6 1.0 ND2 D:ASN260 5.0 63.8 1.0

Magnesium binding site 5 out of 5 in the Structure of the Human Atp Synthase Bound to Bedaquiline (Composite)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of the Human Atp Synthase Bound to Bedaquiline (Composite) within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg502 b:59.1 occ:1.00 O3B F:ADP501 2.1 72.3 1.0 OG1 F:THR166 2.1 65.2 1.0 PB F:ADP501 3.3 72.3 1.0 CB F:THR166 3.5 65.2 1.0 OE2 F:GLU191 3.5 55.0 1.0 O1B F:ADP501 3.5 72.3 1.0 NH2 F:ARG192 3.6 51.5 1.0 O2B F:ADP501 4.1 72.3 1.0 N F:THR166 4.1 65.2 1.0 O1A F:ADP501 4.1 72.3 1.0 OE2 F:GLU195 4.3 57.3 1.0 CA F:THR166 4.3 65.2 1.0 CD F:GLU191 4.4 55.0 1.0 OD2 F:ASP259 4.4 53.6 1.0 CG2 F:THR166 4.4 65.2 1.0 OE1 F:GLU195 4.4 57.3 1.0 O3A F:ADP501 4.5 72.3 1.0 OD1 F:ASP259 4.6 53.6 1.0 CZ F:ARG192 4.7 51.5 1.0 CE F:LYS165 4.7 62.0 1.0 NZ F:LYS165 4.8 62.0 1.0 CD F:GLU195 4.8 57.3 1.0 PA F:ADP501 4.8 72.3 1.0 OE1 F:GLU191 4.8 55.0 1.0 NH1 F:ARG192 4.8 51.5 1.0 CB F:LYS165 4.9 62.0 1.0 CG F:ASP259 5.0 53.6 1.0 O2A F:ADP501 5.0 72.3 1.0

Y.Zhang, Y.Lai, F.Liu, Z.Rao, H.Gong. Structure of Mycobacterium Tuberculosis Atp Synthase To Be Published.