Magnesium in PDB 8hh6: F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp

All present enzymatic activity of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp:
7.1.2.2;

The binding sites of Magnesium atom in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp (pdb code 8hh6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp, PDB code: 8hh6:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:75.7 occ:1.00 OG1 A:THR176 2.0 76.4 1.0 O1G A:ATP600 2.0 84.5 1.0 O1B A:ATP600 3.0 84.5 1.0 CB A:THR176 3.3 76.4 1.0 PG A:ATP600 3.4 84.5 1.0 NE2 A:GLN200 3.6 73.8 1.0 OD1 A:ASP261 3.8 72.8 1.0 CG2 A:THR176 3.9 76.4 1.0 O3B A:ATP600 4.0 84.5 1.0 PB A:ATP600 4.0 84.5 1.0 OD2 A:ASP261 4.0 72.8 1.0 O2A A:ATP600 4.1 84.5 1.0 O2G A:ATP600 4.2 84.5 1.0 CG A:ASP261 4.4 72.8 1.0 CA A:THR176 4.4 76.4 1.0 N A:THR176 4.5 76.4 1.0 O3G A:ATP600 4.5 84.5 1.0 CD A:GLN200 4.7 73.8 1.0 O3A A:ATP600 4.9 84.5 1.0

Magnesium binding site 2 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:76.2 occ:1.00 O2G B:ATP602 2.0 82.6 1.0 OG1 B:THR176 2.0 72.1 1.0 O2B B:ATP602 2.2 82.6 1.0 PG B:ATP602 3.2 82.6 1.0 O3B B:ATP602 3.3 82.6 1.0 PB B:ATP602 3.3 82.6 1.0 CB B:THR176 3.3 72.1 1.0 O1G B:ATP602 4.0 82.6 1.0 CG2 B:THR176 4.1 72.1 1.0 O1B B:ATP602 4.3 82.6 1.0 N B:THR176 4.3 72.1 1.0 O3G B:ATP602 4.3 82.6 1.0 O3A B:ATP602 4.4 82.6 1.0 CA B:THR176 4.4 72.1 1.0 O2A B:ATP602 4.5 82.6 1.0 NE2 B:GLN200 4.6 72.5 1.0 OD2 B:ASP261 4.7 69.2 1.0 PA B:ATP602 4.9 82.6 1.0 OD1 B:ASP261 5.0 69.2 1.0

Magnesium binding site 3 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:62.6 occ:1.00 OG1 C:THR176 2.1 61.9 1.0 O1G C:ATP600 2.1 68.3 1.0 O2B C:ATP600 2.3 68.3 1.0 PG C:ATP600 3.1 68.3 1.0 O3B C:ATP600 3.2 68.3 1.0 CB C:THR176 3.3 61.9 1.0 PB C:ATP600 3.3 68.3 1.0 O2A C:ATP600 4.1 68.3 1.0 O2G C:ATP600 4.1 68.3 1.0 CG2 C:THR176 4.2 61.9 1.0 N C:THR176 4.2 61.9 1.0 O3G C:ATP600 4.3 68.3 1.0 O3A C:ATP600 4.3 68.3 1.0 CA C:THR176 4.3 61.9 1.0 O1B C:ATP600 4.4 68.3 1.0 PA C:ATP600 4.7 68.3 1.0 NE2 C:GLN200 4.7 67.4 1.0 OD1 C:ASP261 4.8 66.5 1.0 O1A C:ATP600 4.9 68.3 1.0

Magnesium binding site 4 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg601 b:67.4 occ:1.00 O2 D:PO4603 2.0 73.7 1.0 OG1 D:THR165 2.0 67.9 1.0 O1B D:ADP602 2.3 71.4 1.0 P D:PO4603 3.4 73.7 1.0 CB D:THR165 3.5 67.9 1.0 PB D:ADP602 3.6 71.4 1.0 O4 D:PO4603 3.8 73.7 1.0 OE1 D:GLU194 3.8 74.1 1.0 N D:THR165 4.1 67.9 1.0 O2B D:ADP602 4.2 71.4 1.0 CG2 D:THR165 4.3 67.9 1.0 CA D:THR165 4.3 67.9 1.0 O3 D:PO4603 4.3 73.7 1.0 O1 D:PO4603 4.3 73.7 1.0 O1A D:ADP602 4.4 71.4 1.0 O3B D:ADP602 4.4 71.4 1.0 OD1 D:ASP252 4.4 72.5 1.0 NH2 D:ARG256 4.4 67.6 1.0 NH1 D:ARG191 4.4 70.6 1.0 OE2 D:GLU194 4.7 74.1 1.0 CD D:GLU194 4.7 74.1 1.0 O3A D:ADP602 4.7 71.4 1.0 PA D:ADP602 4.9 71.4 1.0

Magnesium binding site 5 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:93.2 occ:1.00 OG1 E:THR165 2.1 88.0 1.0 O2B E:ATP501 2.5 95.7 1.0 O2G E:ATP501 2.6 95.7 1.0 PG E:ATP501 3.5 95.7 1.0 CB E:THR165 3.5 88.0 1.0 O3B E:ATP501 3.6 95.7 1.0 PB E:ATP501 3.6 95.7 1.0 O1G E:ATP501 3.9 95.7 1.0 N E:THR165 4.1 88.0 1.0 OE1 E:GLU194 4.2 83.3 1.0 CA E:THR165 4.3 88.0 1.0 CG2 E:THR165 4.4 88.0 1.0 O3A E:ATP501 4.6 95.7 1.0 O1B E:ATP501 4.7 95.7 1.0 O1A E:ATP501 4.7 95.7 1.0 O2A E:ATP501 4.8 95.7 1.0 O3G E:ATP501 4.9 95.7 1.0 PA E:ATP501 4.9 95.7 1.0 CB E:LYS164 5.0 88.4 1.0

Magnesium binding site 6 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of F1 Domain of FOF1-Atpase From Bacillus PS3,Step Waiting,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:65.3 occ:1.00 OG1 F:THR165 2.0 64.6 1.0 O3G F:ATP602 2.1 68.3 1.0 O2B F:ATP602 2.5 68.3 1.0 OE1 F:GLU190 3.3 72.8 1.0 PG F:ATP602 3.4 68.3 1.0 CB F:THR165 3.5 64.6 1.0 PB F:ATP602 3.7 68.3 1.0 O3B F:ATP602 3.7 68.3 1.0 CD F:GLU190 3.8 72.8 1.0 OE2 F:GLU190 3.8 72.8 1.0 O1G F:ATP602 3.9 68.3 1.0 NH1 F:ARG191 4.1 68.2 1.0 CG2 F:THR165 4.2 64.6 1.0 O1A F:ATP602 4.2 68.3 1.0 N F:THR165 4.2 64.6 1.0 CG F:LYS164 4.3 62.5 1.0 CA F:THR165 4.3 64.6 1.0 OE1 F:GLU194 4.4 73.4 1.0 CE F:LYS164 4.4 62.5 1.0 O2G F:ATP602 4.5 68.3 1.0 O3A F:ATP602 4.6 68.3 1.0 O1B F:ATP602 4.7 68.3 1.0 OD1 F:ASP252 4.7 70.6 1.0 NZ F:LYS164 4.8 62.5 1.0 OE2 F:GLU194 4.9 73.4 1.0 CG F:GLU190 5.0 72.8 1.0 CD F:LYS164 5.0 62.5 1.0

A.Nakano, K.Yokoyama, J.Kishikawa, A.Nakanishi, K.Mitsuoka. Rotation Mechanism of Atp Synthases Driven By Atp Hydrolysis To Be Published.