Magnesium in PDB 8hh5: F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,Highatp

All present enzymatic activity of F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,Highatp:
7.1.2.2;

The binding sites of Magnesium atom in the F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,Highatp (pdb code 8hh5). 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 PS3,120 Degrees,Highatp, PDB code: 8hh5:
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 PS3,120 Degrees,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 PS3,120 Degrees,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:81.5 occ:1.00 OG1 A:THR176 2.1 76.9 1.0 O1G A:ATP600 2.2 87.1 1.0 O1B A:ATP600 2.3 87.1 1.0 CB A:THR176 3.2 76.9 1.0 PG A:ATP600 3.4 87.1 1.0 PB A:ATP600 3.5 87.1 1.0 O2A A:ATP600 3.5 87.1 1.0 O3B A:ATP600 3.6 87.1 1.0 CG2 A:THR176 3.8 76.9 1.0 OE1 A:GLN200 3.9 73.2 1.0 O3A A:ATP600 4.3 87.1 1.0 O2G A:ATP600 4.3 87.1 1.0 CA A:THR176 4.5 76.9 1.0 OD2 A:ASP261 4.5 73.9 1.0 PA A:ATP600 4.5 87.1 1.0 O3G A:ATP600 4.6 87.1 1.0 N A:THR176 4.6 76.9 1.0 O2B A:ATP600 4.7 87.1 1.0 CD A:GLN200 4.9 73.2 1.0

Magnesium binding site 2 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,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 PS3,120 Degrees,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:69.7 occ:1.00 OG1 B:THR176 2.0 67.2 1.0 O2G B:ATP602 2.1 77.4 1.0 O2B B:ATP602 2.1 77.4 1.0 CB B:THR176 3.2 67.2 1.0 PG B:ATP602 3.3 77.4 1.0 PB B:ATP602 3.3 77.4 1.0 O3B B:ATP602 3.4 77.4 1.0 NE2 B:GLN200 3.9 67.0 1.0 CG2 B:THR176 4.1 67.2 1.0 O3G B:ATP602 4.1 77.4 1.0 N B:THR176 4.2 67.2 1.0 OD2 B:ASP261 4.2 65.8 1.0 CA B:THR176 4.2 67.2 1.0 O2A B:ATP602 4.3 77.4 1.0 O3A B:ATP602 4.3 77.4 1.0 O1B B:ATP602 4.3 77.4 1.0 O1G B:ATP602 4.4 77.4 1.0 PA B:ATP602 4.7 77.4 1.0 OD1 B:ASP261 4.8 65.8 1.0 O1A B:ATP602 4.9 77.4 1.0 CG B:ASP261 4.9 65.8 1.0 CD B:GLN200 5.0 67.0 1.0

Magnesium binding site 3 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,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 PS3,120 Degrees,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:66.8 occ:1.00 O1G C:ATP600 1.9 68.8 1.0 OG1 C:THR176 2.0 62.2 1.0 O2B C:ATP600 2.1 68.8 1.0 PG C:ATP600 3.0 68.8 1.0 O3B C:ATP600 3.1 68.8 1.0 CB C:THR176 3.2 62.2 1.0 PB C:ATP600 3.2 68.8 1.0 N C:THR176 4.0 62.2 1.0 O2G C:ATP600 4.0 68.8 1.0 O3G C:ATP600 4.1 68.8 1.0 CA C:THR176 4.2 62.2 1.0 CG2 C:THR176 4.2 62.2 1.0 O3A C:ATP600 4.2 68.8 1.0 O1B C:ATP600 4.2 68.8 1.0 O2A C:ATP600 4.3 68.8 1.0 PA C:ATP600 4.6 68.8 1.0 O1A C:ATP600 4.7 68.8 1.0 OD1 C:ASP261 4.8 65.5 1.0 NE2 C:GLN200 4.9 64.8 1.0

Magnesium binding site 4 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,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 PS3,120 Degrees,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg601 b:76.4 occ:1.00 O4 D:PO4602 1.9 77.2 1.0 O1B D:ADP603 2.2 71.5 1.0 OG1 D:THR165 2.3 66.5 1.0 P D:PO4602 3.3 77.2 1.0 PB D:ADP603 3.5 71.5 1.0 O2 D:PO4602 3.7 77.2 1.0 CB D:THR165 3.7 66.5 1.0 OE1 D:GLU194 4.0 73.7 1.0 O3 D:PO4602 4.0 77.2 1.0 O3B D:ADP603 4.2 71.5 1.0 NH1 D:ARG191 4.2 69.4 1.0 O2B D:ADP603 4.2 71.5 1.0 OE2 D:GLU194 4.3 73.7 1.0 N D:THR165 4.3 66.5 1.0 O1 D:PO4602 4.3 77.2 1.0 NH2 D:ARG256 4.4 68.4 1.0 O1A D:ADP603 4.4 71.5 1.0 CA D:THR165 4.5 66.5 1.0 CD D:GLU194 4.5 73.7 1.0 CG2 D:THR165 4.5 66.5 1.0 O3A D:ADP603 4.6 71.5 1.0 NZ D:LYS164 4.9 67.3 1.0 CE D:LYS164 4.9 67.3 1.0 NE C:ARG365 4.9 67.5 1.0 PA D:ADP603 4.9 71.5 1.0

Magnesium binding site 5 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,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 PS3,120 Degrees,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:81.7 occ:1.00 O2G E:ATP501 2.1 93.9 1.0 OG1 E:THR165 2.3 83.2 1.0 O2B E:ATP501 3.2 93.9 1.0 PG E:ATP501 3.5 93.9 1.0 CB E:THR165 3.8 83.2 1.0 O3B E:ATP501 4.1 93.9 1.0 O1G E:ATP501 4.1 93.9 1.0 N E:THR165 4.2 83.2 1.0 PB E:ATP501 4.3 93.9 1.0 OE1 E:GLU194 4.3 80.3 1.0 CA E:THR165 4.5 83.2 1.0 O3G E:ATP501 4.6 93.9 1.0 CG2 E:THR165 4.6 83.2 1.0 O1A E:ATP501 4.8 93.9 1.0 CB E:LYS164 4.9 84.0 1.0

Magnesium binding site 6 out of 6 in the F1 Domain of FOF1-Atpase From Bacillus PS3,120 Degrees,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 PS3,120 Degrees,Highatp within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg601 b:63.7 occ:1.00 O3G F:ATP602 2.0 66.1 1.0 OG1 F:THR165 2.0 62.7 1.0 O2B F:ATP602 2.0 66.1 1.0 PG F:ATP602 3.1 66.1 1.0 OE1 F:GLU190 3.2 67.2 1.0 PB F:ATP602 3.2 66.1 1.0 CB F:THR165 3.3 62.7 1.0 O3B F:ATP602 3.3 66.1 1.0 O1G F:ATP602 3.6 66.1 1.0 O1A F:ATP602 3.8 66.1 1.0 NH1 F:ARG191 4.0 63.9 1.0 O3A F:ATP602 4.1 66.1 1.0 CD F:GLU190 4.1 67.2 1.0 OE2 F:GLU194 4.1 69.9 1.0 N F:THR165 4.2 62.7 1.0 CG2 F:THR165 4.2 62.7 1.0 CA F:THR165 4.3 62.7 1.0 O2G F:ATP602 4.4 66.1 1.0 O1B F:ATP602 4.4 66.1 1.0 OE1 F:GLU194 4.4 69.9 1.0 OE2 F:GLU190 4.4 67.2 1.0 PA F:ATP602 4.5 66.1 1.0 CG F:LYS164 4.5 61.5 1.0 CD F:GLU194 4.7 69.9 1.0 CE F:LYS164 4.8 61.5 1.0 O2A F:ATP602 4.9 66.1 1.0 NZ F:LYS164 4.9 61.5 1.0 NH1 B:ARG365 5.0 63.4 1.0

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