Magnesium in PDB 1ohh: Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
Enzymatic activity of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
All present enzymatic activity of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1:
3.6.1.34;
Protein crystallography data
The structure of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1, PDB code: 1ohh
was solved by
E.Cabezon,
M.G.Montgomery,
A.G.W.Leslie,
J.E.Walker,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.5 /
2.8
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
272.300,
107.200,
152.400,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
23.2 /
28
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
(pdb code 1ohh). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the
Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1, PDB code: 1ohh:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
Magnesium binding site 1 out
of 5 in 1ohh
Go back to
Magnesium Binding Sites List in 1ohh
Magnesium binding site 1 out
of 5 in the Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1512
b:39.8
occ:0.50
|
O2B
|
A:ANP1511
|
2.1
|
39.5
|
0.5
|
O2G
|
A:ANP1511
|
2.1
|
48.1
|
0.5
|
OG1
|
A:THR176
|
2.1
|
67.8
|
0.5
|
PG
|
A:ANP1511
|
3.3
|
53.8
|
0.5
|
CB
|
A:THR176
|
3.3
|
60.1
|
0.5
|
PB
|
A:ANP1511
|
3.4
|
45.6
|
0.5
|
N3B
|
A:ANP1511
|
3.7
|
47.7
|
0.5
|
O3G
|
A:ANP1511
|
3.8
|
47.4
|
0.5
|
OD2
|
A:ASP269
|
4.1
|
70.6
|
0.5
|
OD1
|
A:ASP269
|
4.1
|
70.0
|
0.5
|
O1B
|
A:ANP1511
|
4.2
|
52.1
|
0.5
|
N
|
A:THR176
|
4.2
|
56.2
|
0.5
|
CG2
|
A:THR176
|
4.2
|
61.6
|
0.5
|
CA
|
A:THR176
|
4.3
|
57.9
|
0.5
|
O2A
|
A:ANP1511
|
4.5
|
43.3
|
0.5
|
O3A
|
A:ANP1511
|
4.5
|
48.1
|
0.5
|
CG
|
A:ASP269
|
4.5
|
67.0
|
0.5
|
O1G
|
A:ANP1511
|
4.5
|
52.1
|
0.5
|
PA
|
A:ANP1511
|
4.9
|
49.0
|
0.5
|
|
Magnesium binding site 2 out
of 5 in 1ohh
Go back to
Magnesium Binding Sites List in 1ohh
Magnesium binding site 2 out
of 5 in the Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1512
b:58.0
occ:0.50
|
O2G
|
B:ANP1511
|
2.1
|
55.0
|
0.5
|
O2B
|
B:ANP1511
|
2.2
|
53.6
|
0.5
|
OG1
|
B:THR176
|
2.4
|
42.3
|
0.5
|
PG
|
B:ANP1511
|
3.2
|
51.9
|
0.5
|
PB
|
B:ANP1511
|
3.4
|
55.2
|
0.5
|
CB
|
B:THR176
|
3.5
|
44.4
|
0.5
|
OD2
|
B:ASP269
|
3.6
|
48.8
|
0.5
|
N3B
|
B:ANP1511
|
3.6
|
42.0
|
0.5
|
O1G
|
B:ANP1511
|
3.7
|
47.1
|
0.5
|
N
|
B:THR176
|
3.8
|
44.4
|
0.5
|
OD1
|
B:ASP269
|
4.0
|
54.5
|
0.5
|
CA
|
B:THR176
|
4.1
|
43.0
|
0.5
|
O1B
|
B:ANP1511
|
4.2
|
63.1
|
0.5
|
CG
|
B:ASP269
|
4.2
|
43.8
|
0.5
|
CB
|
B:LYS175
|
4.3
|
41.4
|
0.5
|
NZ
|
B:LYS175
|
4.4
|
46.3
|
0.5
|
O2A
|
B:ANP1511
|
4.4
|
54.5
|
0.5
|
CE
|
B:LYS175
|
4.5
|
38.1
|
0.5
|
O3G
|
B:ANP1511
|
4.5
|
55.3
|
0.5
|
O3A
|
B:ANP1511
|
4.6
|
53.0
|
0.5
|
CG2
|
B:THR176
|
4.7
|
40.8
|
0.5
|
C
|
B:LYS175
|
4.9
|
43.9
|
0.5
|
OE1
|
B:GLN208
|
4.9
|
59.0
|
0.5
|
|
Magnesium binding site 3 out
of 5 in 1ohh
Go back to
Magnesium Binding Sites List in 1ohh
Magnesium binding site 3 out
of 5 in the Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1512
b:47.0
occ:0.50
|
OG1
|
C:THR176
|
2.0
|
33.5
|
0.5
|
O2G
|
C:ANP1511
|
2.1
|
44.3
|
0.5
|
O2B
|
C:ANP1511
|
2.1
|
49.8
|
0.5
|
CB
|
C:THR176
|
3.2
|
38.5
|
0.5
|
PG
|
C:ANP1511
|
3.3
|
43.3
|
0.5
|
PB
|
C:ANP1511
|
3.4
|
48.8
|
0.5
|
N3B
|
C:ANP1511
|
3.7
|
32.7
|
0.5
|
OD1
|
C:ASP269
|
3.8
|
48.1
|
0.5
|
N
|
C:THR176
|
3.9
|
40.2
|
0.5
|
O1B
|
C:ANP1511
|
4.1
|
40.6
|
0.5
|
O3G
|
C:ANP1511
|
4.1
|
42.1
|
0.5
|
CA
|
C:THR176
|
4.1
|
39.7
|
0.5
|
CG2
|
C:THR176
|
4.3
|
38.5
|
0.5
|
O1G
|
C:ANP1511
|
4.4
|
43.6
|
0.5
|
OD2
|
C:ASP269
|
4.4
|
45.2
|
0.5
|
O2A
|
C:ANP1511
|
4.4
|
37.1
|
0.5
|
CG
|
C:ASP269
|
4.5
|
47.7
|
0.5
|
O3A
|
C:ANP1511
|
4.6
|
34.0
|
0.5
|
CB
|
C:LYS175
|
4.7
|
35.3
|
0.5
|
OE1
|
C:GLN208
|
5.0
|
72.0
|
0.5
|
|
Magnesium binding site 4 out
of 5 in 1ohh
Go back to
Magnesium Binding Sites List in 1ohh
Magnesium binding site 4 out
of 5 in the Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1479
b:60.0
occ:0.50
|
OG1
|
D:THR163
|
2.0
|
45.8
|
0.5
|
O2G
|
D:ANP1478
|
2.1
|
61.6
|
0.5
|
O2B
|
D:ANP1478
|
2.2
|
58.6
|
0.5
|
OE1
|
D:GLU188
|
3.1
|
78.5
|
0.5
|
PG
|
D:ANP1478
|
3.2
|
62.7
|
0.5
|
CB
|
D:THR163
|
3.3
|
47.2
|
0.5
|
PB
|
D:ANP1478
|
3.4
|
51.5
|
0.5
|
OE2
|
D:GLU192
|
3.6
|
67.6
|
0.5
|
N3B
|
D:ANP1478
|
3.6
|
61.0
|
0.5
|
O3G
|
D:ANP1478
|
3.9
|
56.1
|
0.5
|
OE1
|
D:GLU192
|
3.9
|
71.5
|
0.5
|
NH1
|
D:ARG189
|
3.9
|
52.9
|
0.5
|
CD
|
D:GLU188
|
4.2
|
76.2
|
0.5
|
O2A
|
D:ANP1478
|
4.2
|
42.5
|
0.5
|
CD
|
D:GLU192
|
4.2
|
66.3
|
0.5
|
N
|
D:THR163
|
4.2
|
51.2
|
0.5
|
OD1
|
D:ASP256
|
4.2
|
50.8
|
0.5
|
CA
|
D:THR163
|
4.3
|
49.2
|
0.5
|
CG2
|
D:THR163
|
4.3
|
47.7
|
0.5
|
O1B
|
D:ANP1478
|
4.4
|
62.4
|
0.5
|
O1G
|
D:ANP1478
|
4.4
|
62.6
|
0.5
|
O3A
|
D:ANP1478
|
4.5
|
46.4
|
0.5
|
OD2
|
D:ASP256
|
4.5
|
52.1
|
0.5
|
NH1
|
C:ARG373
|
4.6
|
65.1
|
0.5
|
CG
|
D:ASP256
|
4.8
|
52.2
|
0.5
|
PA
|
D:ANP1478
|
4.9
|
45.6
|
0.5
|
OE2
|
D:GLU188
|
4.9
|
82.5
|
0.5
|
CE
|
D:LYS162
|
5.0
|
44.4
|
0.5
|
|
Magnesium binding site 5 out
of 5 in 1ohh
Go back to
Magnesium Binding Sites List in 1ohh
Magnesium binding site 5 out
of 5 in the Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Bovine Mitochondrial F1-Atpase Complexed with the Inhibitor Protein IF1 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg1479
b:44.8
occ:0.50
|
O2G
|
F:ANP1478
|
2.1
|
50.7
|
0.5
|
OG1
|
F:THR163
|
2.2
|
41.9
|
0.5
|
O2B
|
F:ANP1478
|
2.2
|
51.8
|
0.5
|
OE1
|
F:GLU188
|
2.8
|
53.0
|
0.5
|
PG
|
F:ANP1478
|
3.4
|
45.8
|
0.5
|
PB
|
F:ANP1478
|
3.4
|
46.1
|
0.5
|
CB
|
F:THR163
|
3.5
|
38.4
|
0.5
|
CD
|
F:GLU188
|
3.6
|
53.6
|
0.5
|
N3B
|
F:ANP1478
|
3.7
|
50.7
|
0.5
|
OD1
|
F:ASP256
|
3.8
|
43.3
|
0.5
|
N
|
F:THR163
|
4.1
|
37.8
|
0.5
|
O1B
|
F:ANP1478
|
4.1
|
57.8
|
0.5
|
O1G
|
F:ANP1478
|
4.1
|
50.7
|
0.5
|
NH1
|
F:ARG189
|
4.2
|
36.2
|
0.5
|
CA
|
F:THR163
|
4.2
|
37.5
|
0.5
|
OD2
|
F:ASP256
|
4.3
|
47.6
|
0.5
|
OE2
|
F:GLU188
|
4.3
|
61.0
|
0.5
|
OE2
|
F:GLU192
|
4.4
|
43.0
|
0.5
|
CE
|
F:LYS162
|
4.4
|
33.0
|
0.5
|
CG
|
F:GLU188
|
4.4
|
34.8
|
0.5
|
CG
|
F:ASP256
|
4.4
|
39.2
|
0.5
|
CG2
|
F:THR163
|
4.5
|
41.5
|
0.5
|
OE1
|
F:GLU192
|
4.5
|
38.7
|
0.5
|
O3G
|
F:ANP1478
|
4.5
|
49.7
|
0.5
|
O2A
|
F:ANP1478
|
4.6
|
54.2
|
0.5
|
O3A
|
F:ANP1478
|
4.6
|
41.7
|
0.5
|
CB
|
F:LYS162
|
4.7
|
25.2
|
0.5
|
ND2
|
F:ASN257
|
4.7
|
41.2
|
0.5
|
NZ
|
F:LYS162
|
4.8
|
26.2
|
0.5
|
CD
|
F:GLU192
|
4.9
|
41.3
|
0.5
|
|
Reference:
E.Cabezon,
M.G.Montgomery,
A.G.W.Leslie,
J.E.Walker.
The Structure of Bovine F1-Atpase in Complex with Its Regulatory Protein IF1 Nat.Struct.Biol. V. 10 744 2003.
ISSN: ISSN 1545-9993
PubMed: 12923572
DOI: 10.1038/NSB966
Page generated: Tue Aug 13 10:39:24 2024
|