Magnesium in PDB 7p0m: Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
Enzymatic activity of Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
All present enzymatic activity of Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains:
3.4.21.53;
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
(pdb code 7p0m). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains, PDB code: 7p0m:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 7p0m
Go back to
Magnesium Binding Sites List in 7p0m
Magnesium binding site 1 out
of 4 in the Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1002
b:100.8
occ:1.00
|
OG1
|
A:THR530
|
2.1
|
103.2
|
1.0
|
O3G
|
A:ATP1001
|
2.1
|
103.0
|
1.0
|
O2B
|
A:ATP1001
|
3.1
|
103.0
|
1.0
|
PG
|
A:ATP1001
|
3.4
|
103.0
|
1.0
|
CB
|
A:THR530
|
3.4
|
103.2
|
1.0
|
O3B
|
A:ATP1001
|
3.5
|
103.0
|
1.0
|
OD2
|
A:ASP590
|
3.6
|
110.5
|
1.0
|
OE2
|
A:GLU591
|
3.9
|
114.1
|
1.0
|
PB
|
A:ATP1001
|
3.9
|
103.0
|
1.0
|
NH2
|
B:ARG652
|
4.1
|
97.8
|
1.0
|
O1A
|
A:ATP1001
|
4.1
|
103.0
|
1.0
|
CG2
|
A:THR530
|
4.2
|
103.2
|
1.0
|
O1G
|
A:ATP1001
|
4.2
|
103.0
|
1.0
|
OG1
|
A:THR638
|
4.2
|
112.7
|
1.0
|
CA
|
A:THR530
|
4.4
|
103.2
|
1.0
|
O2G
|
A:ATP1001
|
4.4
|
103.0
|
1.0
|
CG
|
A:ASP590
|
4.4
|
110.5
|
1.0
|
N
|
A:THR530
|
4.5
|
103.2
|
1.0
|
O3A
|
A:ATP1001
|
4.7
|
103.0
|
1.0
|
CB
|
A:THR638
|
4.8
|
112.7
|
1.0
|
CD
|
A:GLU591
|
5.0
|
114.1
|
1.0
|
PA
|
A:ATP1001
|
5.0
|
103.0
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 7p0m
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Magnesium Binding Sites List in 7p0m
Magnesium binding site 2 out
of 4 in the Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1002
b:90.0
occ:1.00
|
O2G
|
B:ATP1001
|
2.0
|
87.7
|
1.0
|
OG1
|
B:THR530
|
2.1
|
86.3
|
1.0
|
O2B
|
B:ATP1001
|
2.8
|
87.7
|
1.0
|
PG
|
B:ATP1001
|
3.2
|
87.7
|
1.0
|
O3B
|
B:ATP1001
|
3.3
|
87.7
|
1.0
|
CB
|
B:THR530
|
3.4
|
86.3
|
1.0
|
PB
|
B:ATP1001
|
3.7
|
87.7
|
1.0
|
O1G
|
B:ATP1001
|
3.8
|
87.7
|
1.0
|
OG1
|
B:THR638
|
3.8
|
91.0
|
1.0
|
N
|
B:THR530
|
4.1
|
86.3
|
1.0
|
CA
|
B:THR530
|
4.2
|
86.3
|
1.0
|
NH2
|
C:ARG652
|
4.2
|
88.7
|
1.0
|
CB
|
B:THR638
|
4.3
|
91.0
|
1.0
|
CG2
|
B:THR530
|
4.3
|
86.3
|
1.0
|
O3G
|
B:ATP1001
|
4.4
|
87.7
|
1.0
|
OE2
|
B:GLU591
|
4.7
|
98.0
|
1.0
|
O3A
|
B:ATP1001
|
4.7
|
87.7
|
1.0
|
OD1
|
B:ASP590
|
4.7
|
94.1
|
1.0
|
CG2
|
B:THR638
|
4.7
|
91.0
|
1.0
|
O1B
|
B:ATP1001
|
4.8
|
87.7
|
1.0
|
CE
|
B:LYS529
|
4.8
|
84.8
|
1.0
|
CB
|
B:LYS529
|
4.8
|
84.8
|
1.0
|
O1A
|
B:ATP1001
|
5.0
|
87.7
|
1.0
|
C
|
B:LYS529
|
5.0
|
84.8
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 7p0m
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Magnesium Binding Sites List in 7p0m
Magnesium binding site 3 out
of 4 in the Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1002
b:97.4
occ:1.00
|
O2G
|
C:ATP1001
|
2.0
|
96.6
|
1.0
|
OG1
|
C:THR530
|
2.1
|
92.7
|
1.0
|
OE2
|
C:GLU591
|
3.1
|
101.5
|
1.0
|
PG
|
C:ATP1001
|
3.1
|
96.6
|
1.0
|
O2B
|
C:ATP1001
|
3.2
|
96.6
|
1.0
|
CG2
|
C:THR638
|
3.2
|
95.4
|
1.0
|
O1G
|
C:ATP1001
|
3.4
|
96.6
|
1.0
|
CB
|
C:THR530
|
3.5
|
92.7
|
1.0
|
O3B
|
C:ATP1001
|
3.5
|
96.6
|
1.0
|
PB
|
C:ATP1001
|
4.0
|
96.6
|
1.0
|
CB
|
C:THR638
|
4.1
|
95.4
|
1.0
|
CD
|
C:GLU591
|
4.3
|
101.5
|
1.0
|
N
|
C:THR530
|
4.3
|
92.7
|
1.0
|
CG2
|
C:THR530
|
4.3
|
92.7
|
1.0
|
CA
|
C:THR530
|
4.4
|
92.7
|
1.0
|
O3G
|
C:ATP1001
|
4.4
|
96.6
|
1.0
|
OG1
|
C:THR638
|
4.5
|
95.4
|
1.0
|
CB
|
C:ASP590
|
4.7
|
97.6
|
1.0
|
OD1
|
C:ASP590
|
4.8
|
97.6
|
1.0
|
CG
|
C:GLU591
|
4.9
|
101.5
|
1.0
|
O1B
|
C:ATP1001
|
5.0
|
96.6
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 7p0m
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Magnesium Binding Sites List in 7p0m
Magnesium binding site 4 out
of 4 in the Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Human Mitochondrial Lon Protease with Substrate in the Atpase and Protease Domains within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg1002
b:136.8
occ:1.00
|
O2B
|
F:ATP1001
|
2.3
|
129.3
|
1.0
|
OG1
|
F:THR530
|
2.5
|
136.7
|
1.0
|
O2G
|
F:ATP1001
|
2.7
|
129.3
|
1.0
|
OD2
|
F:ASP590
|
3.1
|
152.7
|
1.0
|
PB
|
F:ATP1001
|
3.6
|
129.3
|
1.0
|
CB
|
F:THR530
|
3.6
|
136.7
|
1.0
|
O3B
|
F:ATP1001
|
3.7
|
129.3
|
1.0
|
OD1
|
F:ASP590
|
3.8
|
152.7
|
1.0
|
PG
|
F:ATP1001
|
3.8
|
129.3
|
1.0
|
CG
|
F:ASP590
|
3.8
|
152.7
|
1.0
|
NH2
|
F:ARG546
|
4.2
|
154.6
|
1.0
|
CG2
|
F:THR530
|
4.3
|
136.7
|
1.0
|
O3A
|
F:ATP1001
|
4.4
|
129.3
|
1.0
|
O1A
|
F:ATP1001
|
4.6
|
129.3
|
1.0
|
CZ
|
F:ARG546
|
4.6
|
154.6
|
1.0
|
O3G
|
F:ATP1001
|
4.6
|
129.3
|
1.0
|
O1B
|
F:ATP1001
|
4.6
|
129.3
|
1.0
|
O2A
|
F:ATP1001
|
4.7
|
129.3
|
1.0
|
PA
|
F:ATP1001
|
4.8
|
129.3
|
1.0
|
CA
|
F:THR530
|
4.8
|
136.7
|
1.0
|
N
|
F:THR530
|
4.9
|
136.7
|
1.0
|
NH1
|
F:ARG546
|
4.9
|
154.6
|
1.0
|
O1G
|
F:ATP1001
|
5.0
|
129.3
|
1.0
|
|
Reference:
G.Valentin Gese,
S.Shahzad,
C.Pardo-Hernandez,
A.Wramstedt,
M.Falkenberg,
M.Hallberg.
A Dual Allosteric Pathway Drives Human Mitochondrial Lon To Be Published.
Page generated: Thu Oct 3 03:57:55 2024
|