Magnesium in PDB 7upr: Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation)
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation)
(pdb code 7upr). 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 Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation), PDB code: 7upr:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 7upr
Go back to
Magnesium Binding Sites List in 7upr
Magnesium binding site 1 out
of 4 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg502
b:95.6
occ:1.00
|
O2B
|
C:ATP501
|
2.1
|
98.1
|
1.0
|
OG1
|
C:THR140
|
2.4
|
96.0
|
1.0
|
O3G
|
C:ATP501
|
2.6
|
98.1
|
1.0
|
OD1
|
C:ASP192
|
3.3
|
94.5
|
1.0
|
PB
|
C:ATP501
|
3.5
|
98.1
|
1.0
|
OD2
|
C:ASP192
|
3.6
|
94.5
|
1.0
|
NH2
|
D:ARG250
|
3.8
|
89.4
|
1.0
|
O3B
|
C:ATP501
|
3.8
|
98.1
|
1.0
|
PG
|
C:ATP501
|
3.8
|
98.1
|
1.0
|
CB
|
C:THR140
|
3.8
|
96.0
|
1.0
|
CG
|
C:ASP192
|
3.9
|
94.5
|
1.0
|
O1A
|
C:ATP501
|
4.2
|
98.1
|
1.0
|
CG2
|
C:THR140
|
4.3
|
96.0
|
1.0
|
O1B
|
C:ATP501
|
4.4
|
98.1
|
1.0
|
O3A
|
C:ATP501
|
4.5
|
98.1
|
1.0
|
N
|
C:THR140
|
4.5
|
96.0
|
1.0
|
CA
|
C:THR140
|
4.6
|
96.0
|
1.0
|
OE1
|
C:GLN193
|
4.7
|
91.1
|
1.0
|
O1G
|
C:ATP501
|
4.7
|
98.1
|
1.0
|
PA
|
C:ATP501
|
4.8
|
98.1
|
1.0
|
O
|
D:ASP221
|
4.8
|
98.0
|
1.0
|
O2G
|
C:ATP501
|
4.8
|
98.1
|
1.0
|
O
|
D:MET217
|
4.9
|
90.0
|
1.0
|
O2A
|
C:ATP501
|
5.0
|
98.1
|
1.0
|
CB
|
C:LYS139
|
5.0
|
89.0
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 7upr
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Magnesium Binding Sites List in 7upr
Magnesium binding site 2 out
of 4 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg502
b:101.7
occ:1.00
|
O2B
|
B:ATP501
|
2.1
|
109.7
|
1.0
|
O3G
|
B:ATP501
|
2.1
|
109.7
|
1.0
|
OG1
|
B:THR140
|
2.2
|
111.0
|
1.0
|
O3B
|
B:ATP501
|
2.8
|
109.7
|
1.0
|
PG
|
B:ATP501
|
2.9
|
109.7
|
1.0
|
PB
|
B:ATP501
|
3.0
|
109.7
|
1.0
|
NH2
|
C:ARG250
|
3.5
|
95.1
|
1.0
|
O2G
|
B:ATP501
|
3.5
|
109.7
|
1.0
|
CB
|
B:THR140
|
3.6
|
111.0
|
1.0
|
OE1
|
B:GLN193
|
3.7
|
107.7
|
1.0
|
O3A
|
B:ATP501
|
4.0
|
109.7
|
1.0
|
OD2
|
B:ASP192
|
4.0
|
111.6
|
1.0
|
OD1
|
B:ASP192
|
4.0
|
111.6
|
1.0
|
O1B
|
B:ATP501
|
4.2
|
109.7
|
1.0
|
O1G
|
B:ATP501
|
4.3
|
109.7
|
1.0
|
CG2
|
B:THR140
|
4.3
|
111.0
|
1.0
|
O1A
|
B:ATP501
|
4.4
|
109.7
|
1.0
|
N
|
B:THR140
|
4.4
|
111.0
|
1.0
|
CG
|
B:ASP192
|
4.5
|
111.6
|
1.0
|
CA
|
B:THR140
|
4.5
|
111.0
|
1.0
|
CZ
|
C:ARG250
|
4.7
|
95.1
|
1.0
|
PA
|
B:ATP501
|
4.9
|
109.7
|
1.0
|
CD
|
B:GLN193
|
4.9
|
107.7
|
1.0
|
O
|
C:ASP221
|
4.9
|
107.7
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 7upr
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Magnesium Binding Sites List in 7upr
Magnesium binding site 3 out
of 4 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg502
b:98.2
occ:1.00
|
O2B
|
E:ATP501
|
2.1
|
104.1
|
1.0
|
O3G
|
E:ATP501
|
2.2
|
104.1
|
1.0
|
OG1
|
E:THR140
|
2.4
|
99.1
|
1.0
|
PB
|
E:ATP501
|
3.2
|
104.1
|
1.0
|
O3B
|
E:ATP501
|
3.3
|
104.1
|
1.0
|
PG
|
E:ATP501
|
3.4
|
104.1
|
1.0
|
CB
|
E:THR140
|
3.8
|
99.1
|
1.0
|
O1A
|
E:ATP501
|
3.8
|
104.1
|
1.0
|
NH2
|
F:ARG250
|
3.9
|
99.2
|
1.0
|
O3A
|
E:ATP501
|
4.1
|
104.1
|
1.0
|
O
|
F:ASP221
|
4.1
|
109.7
|
1.0
|
OD1
|
E:ASP192
|
4.1
|
101.3
|
1.0
|
O2G
|
E:ATP501
|
4.3
|
104.1
|
1.0
|
CG2
|
E:THR140
|
4.3
|
99.1
|
1.0
|
OD2
|
E:ASP192
|
4.4
|
101.3
|
1.0
|
PA
|
E:ATP501
|
4.4
|
104.1
|
1.0
|
O1B
|
E:ATP501
|
4.4
|
104.1
|
1.0
|
O1G
|
E:ATP501
|
4.5
|
104.1
|
1.0
|
OE1
|
E:GLN193
|
4.6
|
98.0
|
1.0
|
CG
|
E:ASP192
|
4.7
|
101.3
|
1.0
|
NH1
|
F:ARG250
|
4.7
|
99.2
|
1.0
|
CA
|
E:THR140
|
4.8
|
99.1
|
1.0
|
O2A
|
E:ATP501
|
4.8
|
104.1
|
1.0
|
N
|
E:THR140
|
4.8
|
99.1
|
1.0
|
CZ
|
F:ARG250
|
4.8
|
99.2
|
1.0
|
OD1
|
F:ASP221
|
5.0
|
109.7
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 7upr
Go back to
Magnesium Binding Sites List in 7upr
Magnesium binding site 4 out
of 4 in the Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Human Mitochondrial Aaa Protein ATAD1 (with A Catalytic Dead Mutation) in Complex with A Peptide Substrate (Closed Conformation) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg502
b:100.5
occ:1.00
|
O2B
|
D:ATP501
|
2.1
|
98.6
|
1.0
|
O3G
|
D:ATP501
|
2.5
|
98.6
|
1.0
|
OG1
|
D:THR140
|
2.6
|
92.8
|
1.0
|
PB
|
D:ATP501
|
3.4
|
98.6
|
1.0
|
OD2
|
D:ASP192
|
3.5
|
92.3
|
1.0
|
NH2
|
E:ARG250
|
3.5
|
89.7
|
1.0
|
OD1
|
D:ASP192
|
3.6
|
92.3
|
1.0
|
O3B
|
D:ATP501
|
3.6
|
98.6
|
1.0
|
PG
|
D:ATP501
|
3.7
|
98.6
|
1.0
|
CG
|
D:ASP192
|
3.9
|
92.3
|
1.0
|
CB
|
D:THR140
|
4.0
|
92.8
|
1.0
|
OE1
|
D:GLN193
|
4.1
|
92.3
|
1.0
|
O1A
|
D:ATP501
|
4.1
|
98.6
|
1.0
|
O3A
|
D:ATP501
|
4.3
|
98.6
|
1.0
|
O1B
|
D:ATP501
|
4.4
|
98.6
|
1.0
|
CG2
|
D:THR140
|
4.5
|
92.8
|
1.0
|
O2G
|
D:ATP501
|
4.5
|
98.6
|
1.0
|
PA
|
D:ATP501
|
4.7
|
98.6
|
1.0
|
O
|
E:MET217
|
4.7
|
87.9
|
1.0
|
N
|
D:THR140
|
4.8
|
92.8
|
1.0
|
O
|
E:ASP221
|
4.8
|
98.5
|
1.0
|
CA
|
D:THR140
|
4.8
|
92.8
|
1.0
|
O1G
|
D:ATP501
|
4.8
|
98.6
|
1.0
|
CZ
|
E:ARG250
|
4.8
|
89.7
|
1.0
|
CA
|
E:GLY222
|
5.0
|
104.6
|
1.0
|
O2A
|
D:ATP501
|
5.0
|
98.6
|
1.0
|
|
Reference:
L.Wang,
H.Toutkoushian,
V.Belyy,
C.Y.Kokontis,
P.Walter.
Conserved Structural Elements Specialize ATAD1 As A Membrane Protein Extraction Machine. Elife V. 11 2022.
ISSN: ESSN 2050-084X
PubMed: 35550246
DOI: 10.7554/ELIFE.73941
Page generated: Thu Oct 3 10:09:29 2024
|