Magnesium in PDB 8hh1: FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
Enzymatic activity of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
All present enzymatic activity of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp:
7.1.2.2;
Magnesium Binding Sites:
The binding sites of Magnesium atom in the FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
(pdb code 8hh1). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the
FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp, PDB code: 8hh1:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
Magnesium binding site 1 out
of 5 in 8hh1
Go back to
Magnesium Binding Sites List in 8hh1
Magnesium binding site 1 out
of 5 in the FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg601
b:52.4
occ:1.00
|
OG1
|
A:THR176
|
2.0
|
50.5
|
1.0
|
O1G
|
A:ATP600
|
2.1
|
57.1
|
1.0
|
O1B
|
A:ATP600
|
2.2
|
57.1
|
1.0
|
PG
|
A:ATP600
|
3.2
|
57.1
|
1.0
|
PB
|
A:ATP600
|
3.3
|
57.1
|
1.0
|
CB
|
A:THR176
|
3.3
|
50.5
|
1.0
|
O3B
|
A:ATP600
|
3.4
|
57.1
|
1.0
|
O2A
|
A:ATP600
|
3.7
|
57.1
|
1.0
|
O3G
|
A:ATP600
|
3.9
|
57.1
|
1.0
|
CG2
|
A:THR176
|
4.0
|
50.5
|
1.0
|
O3A
|
A:ATP600
|
4.2
|
57.1
|
1.0
|
N
|
A:THR176
|
4.3
|
50.5
|
1.0
|
OD1
|
A:ASP261
|
4.4
|
51.9
|
1.0
|
CA
|
A:THR176
|
4.4
|
50.5
|
1.0
|
O2B
|
A:ATP600
|
4.5
|
57.1
|
1.0
|
O2G
|
A:ATP600
|
4.5
|
57.1
|
1.0
|
OD2
|
A:ASP261
|
4.6
|
51.9
|
1.0
|
PA
|
A:ATP600
|
4.6
|
57.1
|
1.0
|
NH2
|
D:ARG352
|
4.8
|
59.4
|
1.0
|
CG
|
A:ASP261
|
4.9
|
51.9
|
1.0
|
|
Magnesium binding site 2 out
of 5 in 8hh1
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Magnesium Binding Sites List in 8hh1
Magnesium binding site 2 out
of 5 in the FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg601
b:57.7
occ:1.00
|
O2G
|
B:ATP600
|
2.0
|
60.0
|
1.0
|
OG1
|
B:THR176
|
2.1
|
52.6
|
1.0
|
O2B
|
B:ATP600
|
2.5
|
60.0
|
1.0
|
CB
|
B:THR176
|
3.3
|
52.6
|
1.0
|
PG
|
B:ATP600
|
3.4
|
60.0
|
1.0
|
O3B
|
B:ATP600
|
3.7
|
60.0
|
1.0
|
O2A
|
B:ATP600
|
3.7
|
60.0
|
1.0
|
PB
|
B:ATP600
|
3.7
|
60.0
|
1.0
|
CG2
|
B:THR176
|
3.9
|
52.6
|
1.0
|
OD1
|
B:ASP261
|
4.0
|
50.7
|
1.0
|
OE1
|
B:GLN200
|
4.2
|
54.0
|
1.0
|
O1G
|
B:ATP600
|
4.3
|
60.0
|
1.0
|
O3G
|
B:ATP600
|
4.4
|
60.0
|
1.0
|
CA
|
B:THR176
|
4.5
|
52.6
|
1.0
|
OD2
|
B:ASP261
|
4.5
|
50.7
|
1.0
|
N
|
B:THR176
|
4.6
|
52.6
|
1.0
|
O3A
|
B:ATP600
|
4.6
|
60.0
|
1.0
|
CG
|
B:ASP261
|
4.7
|
50.7
|
1.0
|
PA
|
B:ATP600
|
4.8
|
60.0
|
1.0
|
O1B
|
B:ATP600
|
4.8
|
60.0
|
1.0
|
|
Magnesium binding site 3 out
of 5 in 8hh1
Go back to
Magnesium Binding Sites List in 8hh1
Magnesium binding site 3 out
of 5 in the FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg601
b:48.7
occ:1.00
|
OG1
|
C:THR176
|
2.0
|
47.8
|
1.0
|
O1G
|
C:ATP600
|
2.1
|
52.7
|
1.0
|
O2B
|
C:ATP600
|
2.3
|
52.7
|
1.0
|
PG
|
C:ATP600
|
3.2
|
52.7
|
1.0
|
CB
|
C:THR176
|
3.3
|
47.8
|
1.0
|
O3B
|
C:ATP600
|
3.4
|
52.7
|
1.0
|
PB
|
C:ATP600
|
3.4
|
52.7
|
1.0
|
CG2
|
C:THR176
|
4.0
|
47.8
|
1.0
|
OD2
|
C:ASP261
|
4.1
|
48.9
|
1.0
|
O2G
|
C:ATP600
|
4.1
|
52.7
|
1.0
|
N
|
C:THR176
|
4.3
|
47.8
|
1.0
|
CA
|
C:THR176
|
4.4
|
47.8
|
1.0
|
O3A
|
C:ATP600
|
4.4
|
52.7
|
1.0
|
O3G
|
C:ATP600
|
4.4
|
52.7
|
1.0
|
O2A
|
C:ATP600
|
4.4
|
52.7
|
1.0
|
O1B
|
C:ATP600
|
4.5
|
52.7
|
1.0
|
PA
|
C:ATP600
|
4.8
|
52.7
|
1.0
|
O1A
|
C:ATP600
|
4.8
|
52.7
|
1.0
|
|
Magnesium binding site 4 out
of 5 in 8hh1
Go back to
Magnesium Binding Sites List in 8hh1
Magnesium binding site 4 out
of 5 in the FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg601
b:61.4
occ:1.00
|
OG1
|
D:THR165
|
1.7
|
55.5
|
1.0
|
O1G
|
D:ATP602
|
1.8
|
60.3
|
1.0
|
O1B
|
D:ATP602
|
2.4
|
60.3
|
1.0
|
PG
|
D:ATP602
|
2.8
|
60.3
|
1.0
|
CB
|
D:THR165
|
3.0
|
55.5
|
1.0
|
O3B
|
D:ATP602
|
3.1
|
60.3
|
1.0
|
PB
|
D:ATP602
|
3.2
|
60.3
|
1.0
|
O1A
|
D:ATP602
|
3.2
|
60.3
|
1.0
|
OE2
|
D:GLU194
|
3.4
|
56.8
|
1.0
|
O2G
|
D:ATP602
|
3.4
|
60.3
|
1.0
|
O3A
|
D:ATP602
|
3.7
|
60.3
|
1.0
|
CG2
|
D:THR165
|
3.9
|
55.5
|
1.0
|
N
|
D:THR165
|
3.9
|
55.5
|
1.0
|
PA
|
D:ATP602
|
4.0
|
60.3
|
1.0
|
NH1
|
D:ARG191
|
4.0
|
53.3
|
1.0
|
CA
|
D:THR165
|
4.0
|
55.5
|
1.0
|
O3G
|
D:ATP602
|
4.1
|
60.3
|
1.0
|
CD
|
D:GLU194
|
4.2
|
56.8
|
1.0
|
OE1
|
D:GLU194
|
4.2
|
56.8
|
1.0
|
OE1
|
D:GLU190
|
4.2
|
54.8
|
1.0
|
O2A
|
D:ATP602
|
4.6
|
60.3
|
1.0
|
O2B
|
D:ATP602
|
4.6
|
60.3
|
1.0
|
|
Magnesium binding site 5 out
of 5 in 8hh1
Go back to
Magnesium Binding Sites List in 8hh1
Magnesium binding site 5 out
of 5 in the FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of FOF1-Atpase From Bacillus PS3, 81 Degrees, Highatp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg601
b:53.3
occ:1.00
|
OG1
|
F:THR165
|
2.0
|
49.9
|
1.0
|
O3G
|
F:ATP602
|
2.1
|
52.8
|
1.0
|
O2B
|
F:ATP602
|
2.2
|
52.8
|
1.0
|
OE1
|
F:GLU190
|
3.1
|
54.4
|
1.0
|
CB
|
F:THR165
|
3.4
|
49.9
|
1.0
|
PG
|
F:ATP602
|
3.4
|
52.8
|
1.0
|
PB
|
F:ATP602
|
3.5
|
52.8
|
1.0
|
O3B
|
F:ATP602
|
3.6
|
52.8
|
1.0
|
NH1
|
F:ARG191
|
4.0
|
50.6
|
1.0
|
OE1
|
F:GLU194
|
4.1
|
55.8
|
1.0
|
N
|
F:THR165
|
4.1
|
49.9
|
1.0
|
CD
|
F:GLU190
|
4.2
|
54.4
|
1.0
|
OE2
|
F:GLU194
|
4.2
|
55.8
|
1.0
|
O1G
|
F:ATP602
|
4.3
|
52.8
|
1.0
|
CA
|
F:THR165
|
4.3
|
49.9
|
1.0
|
CG2
|
F:THR165
|
4.3
|
49.9
|
1.0
|
O1B
|
F:ATP602
|
4.5
|
52.8
|
1.0
|
O3A
|
F:ATP602
|
4.5
|
52.8
|
1.0
|
O2G
|
F:ATP602
|
4.5
|
52.8
|
1.0
|
O1A
|
F:ATP602
|
4.5
|
52.8
|
1.0
|
CD
|
F:GLU194
|
4.6
|
55.8
|
1.0
|
OE2
|
F:GLU190
|
4.6
|
54.4
|
1.0
|
OD1
|
F:ASP252
|
4.9
|
52.4
|
1.0
|
PA
|
F:ATP602
|
4.9
|
52.8
|
1.0
|
CE
|
F:LYS164
|
5.0
|
47.5
|
1.0
|
CB
|
F:LYS164
|
5.0
|
47.5
|
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 Jul 28 00:47:17 2023
|