Magnesium in PDB 8hhc: F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp

Enzymatic activity of F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp

All present enzymatic activity of F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp:
7.1.2.2;

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 5 in 8hhc

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Magnesium binding site 1 out of 5 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp


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,Post-Hyd',Lowatp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:119.2
occ:1.00
O1G A:ATP601 2.0 128.6 1.0
OG1 A:THR176 2.9 108.4 1.0
PG A:ATP601 3.3 128.6 1.0
O2G A:ATP601 3.7 128.6 1.0
O1B A:ATP601 3.8 128.6 1.0
OE1 A:GLN200 4.1 82.3 1.0
O3B A:ATP601 4.2 128.6 1.0
CB A:THR176 4.3 108.4 1.0
OE2 A:GLU320 4.3 101.1 1.0
O3G A:ATP601 4.5 128.6 1.0
O A:ASP261 4.6 81.8 1.0
CD A:GLN200 4.6 82.3 1.0
PB A:ATP601 4.7 128.6 1.0
CE A:LYS175 4.7 105.5 1.0
NZ A:LYS175 4.7 105.5 1.0
N A:THR176 4.8 108.4 1.0
CB A:ASP261 4.9 81.8 1.0
CG2 A:THR176 4.9 108.4 1.0
CA A:THR176 5.0 108.4 1.0
CG A:GLN200 5.0 82.3 1.0
CD2 A:PHE318 5.0 82.9 1.0

Magnesium binding site 2 out of 5 in 8hhc

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Magnesium binding site 2 out of 5 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp


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,Post-Hyd',Lowatp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:104.5
occ:1.00
O2B B:ATP600 2.1 105.0 1.0
O2G B:ATP600 2.2 105.0 1.0
OG1 B:THR176 2.2 82.0 1.0
O3B B:ATP600 2.3 105.0 1.0
PG B:ATP600 2.4 105.0 1.0
O1G B:ATP600 2.6 105.0 1.0
PB B:ATP600 2.7 105.0 1.0
O2A B:ATP600 2.8 105.0 1.0
CB B:THR176 3.3 82.0 1.0
O3A B:ATP600 3.4 105.0 1.0
N B:THR176 3.8 82.0 1.0
PA B:ATP600 3.8 105.0 1.0
O3G B:ATP600 3.9 105.0 1.0
O1B B:ATP600 3.9 105.0 1.0
CA B:THR176 4.2 82.0 1.0
CG2 B:THR176 4.4 82.0 1.0
O1A B:ATP600 4.6 105.0 1.0
N B:LYS175 4.8 79.4 1.0
C B:LYS175 4.9 79.4 1.0
OE1 B:GLN200 4.9 67.8 1.0
CB B:LYS175 4.9 79.4 1.0
O5' B:ATP600 4.9 105.0 1.0

Magnesium binding site 3 out of 5 in 8hhc

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Magnesium binding site 3 out of 5 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp


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,Post-Hyd',Lowatp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:77.4
occ:1.00
O2B C:ATP600 2.0 81.1 1.0
OG1 C:THR176 2.0 72.7 1.0
O1G C:ATP600 2.0 81.1 1.0
PB C:ATP600 3.1 81.1 1.0
PG C:ATP600 3.2 81.1 1.0
O3B C:ATP600 3.3 81.1 1.0
CB C:THR176 3.3 72.7 1.0
O1B C:ATP600 4.0 81.1 1.0
N C:THR176 4.0 72.7 1.0
O3G C:ATP600 4.2 81.1 1.0
CG2 C:THR176 4.2 72.7 1.0
O2G C:ATP600 4.2 81.1 1.0
CA C:THR176 4.3 72.7 1.0
O3A C:ATP600 4.3 81.1 1.0
O2A C:ATP600 4.5 81.1 1.0
OD2 C:ASP261 4.6 71.0 1.0
NE2 C:GLN200 4.7 72.0 1.0
OD1 C:ASP261 4.7 71.0 1.0
PA C:ATP600 4.9 81.1 1.0
NZ C:LYS175 5.0 72.2 1.0

Magnesium binding site 4 out of 5 in 8hhc

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Magnesium binding site 4 out of 5 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp


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,Post-Hyd',Lowatp within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg502

b:111.3
occ:1.00
OG1 D:THR165 1.8 108.1 1.0
O3B D:ATP501 2.0 117.2 1.0
PG D:ATP501 2.2 117.2 1.0
O3G D:ATP501 2.2 117.2 1.0
O1G D:ATP501 2.4 117.2 1.0
CB D:THR165 3.1 108.1 1.0
PB D:ATP501 3.4 117.2 1.0
O3A D:ATP501 3.6 117.2 1.0
OE2 D:GLU194 3.6 91.5 1.0
O2G D:ATP501 3.6 117.2 1.0
N D:THR165 3.7 108.1 1.0
O1A D:ATP501 3.7 117.2 1.0
CA D:THR165 3.9 108.1 1.0
PA D:ATP501 4.1 117.2 1.0
CG2 D:THR165 4.1 108.1 1.0
O2B D:ATP501 4.1 117.2 1.0
OD2 D:ASP252 4.3 91.3 1.0
O1B D:ATP501 4.4 117.2 1.0
NH1 D:ARG191 4.4 87.8 1.0
OE2 D:GLU190 4.5 93.9 1.0
O2A D:ATP501 4.5 117.2 1.0
OD1 D:ASP252 4.6 91.3 1.0
CD D:GLU194 4.6 91.5 1.0
C D:LYS164 4.7 109.0 1.0
CB D:LYS164 4.8 109.0 1.0
NH1 C:ARG365 4.8 88.5 1.0
OE1 D:GLU194 4.9 91.5 1.0
CG D:ASP252 4.9 91.3 1.0
ND2 D:ASN253 4.9 93.4 1.0
NZ D:LYS164 5.0 109.0 1.0

Magnesium binding site 5 out of 5 in 8hhc

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Magnesium binding site 5 out of 5 in the F1 Domain of FOF1-Atpase From Bacillus PS3,Post-Hyd',Lowatp


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,Post-Hyd',Lowatp within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg601

b:71.8
occ:1.00
O3G F:ATP602 1.9 70.0 1.0
OG1 F:THR165 2.0 65.9 1.0
OE2 F:GLU194 2.5 73.8 1.0
OE1 F:GLU190 2.9 71.8 1.0
CB F:THR165 2.9 65.9 1.0
NH1 F:ARG191 3.0 68.4 1.0
PG F:ATP602 3.2 70.0 1.0
CD F:GLU194 3.2 73.8 1.0
OE1 F:GLU194 3.2 73.8 1.0
CG2 F:THR165 3.4 65.9 1.0
O2G F:ATP602 3.5 70.0 1.0
O2B F:ATP602 3.6 70.0 1.0
O3B F:ATP602 3.7 70.0 1.0
CD F:GLU190 4.1 71.8 1.0
O1A F:ATP602 4.1 70.0 1.0
CA F:THR165 4.3 65.9 1.0
PB F:ATP602 4.3 70.0 1.0
CZ F:ARG191 4.3 68.4 1.0
O1G F:ATP602 4.4 70.0 1.0
N F:THR165 4.6 65.9 1.0
O3A F:ATP602 4.6 70.0 1.0
CG F:GLU194 4.7 73.8 1.0
OE2 F:GLU190 4.7 71.8 1.0
NH1 B:ARG365 4.7 74.0 1.0
PA F:ATP602 4.7 70.0 1.0
O2A F:ATP602 4.7 70.0 1.0
NH2 F:ARG191 5.0 68.4 1.0

Reference:

A.Nakano, K.Yokoyama, J.Kishikawa, K.Mitsuoka. Rotation Mechanism of Atp Synthases Driven By Atp Hydrolysis To Be Published.
Page generated: Fri Oct 4 04:58:29 2024

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