Magnesium in PDB 7rkh: Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Enzymatic activity of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
All present enzymatic activity of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH:
6.3.4.2;
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
(pdb code 7rkh). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH, PDB code: 7rkh:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 7rkh
Go back to
Magnesium Binding Sites List in 7rkh
Magnesium binding site 1 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg603
b:30.0
occ:1.00
|
OD2
|
D:ASP70
|
1.9
|
31.5
|
1.0
|
OD1
|
D:ASP70
|
2.4
|
31.5
|
1.0
|
CG
|
D:ASP70
|
2.4
|
31.5
|
1.0
|
O1B
|
D:ATP602
|
2.9
|
43.5
|
1.0
|
O3G
|
D:ATP602
|
3.0
|
43.5
|
1.0
|
HZ1
|
D:LYS16
|
3.1
|
26.8
|
1.0
|
OE2
|
D:GLU146
|
3.2
|
21.2
|
1.0
|
HA3
|
D:GLY17
|
3.3
|
37.3
|
1.0
|
HZ2
|
D:LYS16
|
3.4
|
26.8
|
1.0
|
H
|
D:GLY17
|
3.4
|
37.3
|
1.0
|
HZ3
|
D:LYS16
|
3.4
|
26.8
|
1.0
|
HZ3
|
D:LYS38
|
3.5
|
19.4
|
1.0
|
OE1
|
D:GLU146
|
3.5
|
21.2
|
1.0
|
HE3
|
D:LYS38
|
3.5
|
19.4
|
1.0
|
NZ
|
D:LYS16
|
3.6
|
26.8
|
1.0
|
CD
|
D:GLU146
|
3.7
|
21.2
|
1.0
|
O3B
|
D:ATP602
|
3.8
|
43.5
|
1.0
|
CB
|
D:ASP70
|
3.9
|
31.5
|
1.0
|
N
|
D:GLY17
|
3.9
|
37.3
|
1.0
|
HB2
|
D:LYS16
|
3.9
|
26.8
|
1.0
|
PB
|
D:ATP602
|
3.9
|
43.5
|
1.0
|
CA
|
D:GLY17
|
4.0
|
37.3
|
1.0
|
PG
|
D:ATP602
|
4.0
|
43.5
|
1.0
|
O2A
|
D:ATP602
|
4.0
|
43.5
|
1.0
|
HB3
|
D:ASP70
|
4.1
|
31.5
|
1.0
|
HA2
|
D:GLY17
|
4.1
|
37.3
|
1.0
|
NZ
|
D:LYS38
|
4.2
|
19.4
|
1.0
|
HD3
|
D:LYS38
|
4.2
|
19.4
|
1.0
|
CE
|
D:LYS38
|
4.3
|
19.4
|
1.0
|
HB2
|
D:ASP70
|
4.4
|
31.5
|
1.0
|
O4
|
D:UTP601
|
4.4
|
33.3
|
1.0
|
O1A
|
D:ATP602
|
4.5
|
43.5
|
1.0
|
HZ1
|
D:LYS38
|
4.5
|
19.4
|
1.0
|
PA
|
D:ATP602
|
4.5
|
43.5
|
1.0
|
O3A
|
D:ATP602
|
4.6
|
43.5
|
1.0
|
OD2
|
D:ASP68
|
4.6
|
39.0
|
1.0
|
HH
|
D:TYR74
|
4.6
|
28.7
|
1.0
|
HD13
|
D:LEU69
|
4.7
|
38.0
|
1.0
|
HA
|
D:ASP70
|
4.7
|
37.3
|
1.0
|
CD
|
D:LYS38
|
4.8
|
19.4
|
1.0
|
CA
|
D:ASP70
|
4.9
|
37.3
|
1.0
|
O2G
|
D:ATP602
|
4.9
|
43.5
|
1.0
|
C
|
D:LYS16
|
4.9
|
37.3
|
1.0
|
CB
|
D:LYS16
|
5.0
|
26.8
|
1.0
|
H
|
D:ASP70
|
5.0
|
37.3
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 7rkh
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Magnesium Binding Sites List in 7rkh
Magnesium binding site 2 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg604
b:30.0
occ:1.00
|
HZ3
|
D:LYS227
|
2.9
|
47.3
|
1.0
|
O1B
|
C:UTP602
|
3.0
|
33.3
|
1.0
|
O2A
|
C:UTP602
|
3.1
|
33.3
|
1.0
|
O3B
|
C:UTP602
|
3.1
|
33.3
|
1.0
|
O3A
|
C:UTP602
|
3.1
|
33.3
|
1.0
|
PB
|
C:UTP602
|
3.3
|
33.3
|
1.0
|
HZ1
|
D:LYS227
|
3.6
|
47.3
|
1.0
|
NZ
|
D:LYS227
|
3.7
|
47.3
|
1.0
|
PA
|
C:UTP602
|
3.7
|
33.3
|
1.0
|
O3G
|
C:UTP602
|
3.7
|
33.3
|
1.0
|
HZ3
|
D:LYS191
|
3.9
|
41.5
|
1.0
|
PG
|
C:UTP602
|
3.9
|
33.3
|
1.0
|
HZ2
|
D:LYS227
|
3.9
|
47.3
|
1.0
|
HE2
|
C:HIS55
|
4.1
|
59.4
|
1.0
|
C5'
|
C:UTP602
|
4.2
|
33.3
|
1.0
|
O1G
|
C:UTP602
|
4.2
|
33.3
|
1.0
|
HZ2
|
D:LYS191
|
4.2
|
41.5
|
1.0
|
O5'
|
C:UTP602
|
4.2
|
33.3
|
1.0
|
NZ
|
D:LYS191
|
4.6
|
41.5
|
1.0
|
HG
|
C:SER12
|
4.6
|
42.8
|
1.0
|
NE2
|
C:HIS55
|
4.8
|
59.4
|
1.0
|
O2B
|
C:UTP602
|
4.8
|
33.3
|
1.0
|
HD2
|
C:HIS55
|
4.9
|
59.4
|
1.0
|
CE
|
D:LYS227
|
4.9
|
47.3
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 7rkh
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Magnesium Binding Sites List in 7rkh
Magnesium binding site 3 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg603
b:30.0
occ:1.00
|
OD2
|
A:ASP70
|
1.9
|
31.5
|
1.0
|
OD1
|
A:ASP70
|
2.4
|
31.5
|
1.0
|
CG
|
A:ASP70
|
2.4
|
31.5
|
1.0
|
O1B
|
A:ATP602
|
2.9
|
43.5
|
1.0
|
O3G
|
A:ATP602
|
3.0
|
43.5
|
1.0
|
HZ1
|
A:LYS16
|
3.1
|
26.8
|
1.0
|
OE2
|
A:GLU146
|
3.2
|
21.2
|
1.0
|
HA3
|
A:GLY17
|
3.3
|
37.3
|
1.0
|
HZ2
|
A:LYS16
|
3.4
|
26.8
|
1.0
|
H
|
A:GLY17
|
3.4
|
37.3
|
1.0
|
HZ3
|
A:LYS16
|
3.4
|
26.8
|
1.0
|
HZ3
|
A:LYS38
|
3.5
|
19.4
|
1.0
|
OE1
|
A:GLU146
|
3.5
|
21.2
|
1.0
|
HE3
|
A:LYS38
|
3.5
|
19.4
|
1.0
|
NZ
|
A:LYS16
|
3.6
|
26.8
|
1.0
|
CD
|
A:GLU146
|
3.7
|
21.2
|
1.0
|
O3B
|
A:ATP602
|
3.8
|
43.5
|
1.0
|
CB
|
A:ASP70
|
3.9
|
31.5
|
1.0
|
N
|
A:GLY17
|
3.9
|
37.3
|
1.0
|
HB2
|
A:LYS16
|
3.9
|
26.8
|
1.0
|
PB
|
A:ATP602
|
3.9
|
43.5
|
1.0
|
CA
|
A:GLY17
|
4.0
|
37.3
|
1.0
|
PG
|
A:ATP602
|
4.0
|
43.5
|
1.0
|
O2A
|
A:ATP602
|
4.0
|
43.5
|
1.0
|
HB3
|
A:ASP70
|
4.1
|
31.5
|
1.0
|
HA2
|
A:GLY17
|
4.1
|
37.3
|
1.0
|
NZ
|
A:LYS38
|
4.2
|
19.4
|
1.0
|
HD3
|
A:LYS38
|
4.2
|
19.4
|
1.0
|
CE
|
A:LYS38
|
4.3
|
19.4
|
1.0
|
HB2
|
A:ASP70
|
4.4
|
31.5
|
1.0
|
O4
|
A:UTP601
|
4.4
|
33.3
|
1.0
|
O1A
|
A:ATP602
|
4.5
|
43.5
|
1.0
|
HZ1
|
A:LYS38
|
4.5
|
19.4
|
1.0
|
PA
|
A:ATP602
|
4.5
|
43.5
|
1.0
|
O3A
|
A:ATP602
|
4.6
|
43.5
|
1.0
|
OD2
|
A:ASP68
|
4.6
|
39.0
|
1.0
|
HH
|
A:TYR74
|
4.6
|
28.7
|
1.0
|
HD13
|
A:LEU69
|
4.7
|
38.0
|
1.0
|
HA
|
A:ASP70
|
4.7
|
37.3
|
1.0
|
CD
|
A:LYS38
|
4.8
|
19.4
|
1.0
|
CA
|
A:ASP70
|
4.9
|
37.3
|
1.0
|
O2G
|
A:ATP602
|
4.9
|
43.5
|
1.0
|
C
|
A:LYS16
|
4.9
|
37.3
|
1.0
|
CB
|
A:LYS16
|
5.0
|
26.8
|
1.0
|
H
|
A:ASP70
|
5.0
|
37.3
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 7rkh
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Magnesium Binding Sites List in 7rkh
Magnesium binding site 4 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg604
b:30.0
occ:1.00
|
HZ3
|
A:LYS227
|
2.9
|
47.3
|
1.0
|
O2B
|
B:UTP602
|
3.0
|
33.3
|
1.0
|
O1A
|
B:UTP602
|
3.1
|
33.3
|
1.0
|
O3B
|
B:UTP602
|
3.1
|
33.3
|
1.0
|
O3A
|
B:UTP602
|
3.1
|
33.3
|
1.0
|
PB
|
B:UTP602
|
3.3
|
33.3
|
1.0
|
HZ1
|
A:LYS227
|
3.6
|
47.3
|
1.0
|
NZ
|
A:LYS227
|
3.7
|
47.3
|
1.0
|
PA
|
B:UTP602
|
3.7
|
33.3
|
1.0
|
O2G
|
B:UTP602
|
3.7
|
33.3
|
1.0
|
HZ3
|
A:LYS191
|
3.9
|
41.5
|
1.0
|
PG
|
B:UTP602
|
3.9
|
33.3
|
1.0
|
HZ2
|
A:LYS227
|
3.9
|
47.3
|
1.0
|
HE2
|
B:HIS55
|
4.1
|
59.4
|
1.0
|
C5'
|
B:UTP602
|
4.2
|
33.3
|
1.0
|
O1G
|
B:UTP602
|
4.2
|
33.3
|
1.0
|
HZ2
|
A:LYS191
|
4.2
|
41.5
|
1.0
|
O5'
|
B:UTP602
|
4.2
|
33.3
|
1.0
|
NZ
|
A:LYS191
|
4.6
|
41.5
|
1.0
|
HG
|
B:SER12
|
4.6
|
42.8
|
1.0
|
NE2
|
B:HIS55
|
4.8
|
59.4
|
1.0
|
O1B
|
B:UTP602
|
4.8
|
33.3
|
1.0
|
HD2
|
B:HIS55
|
4.9
|
59.4
|
1.0
|
CE
|
A:LYS227
|
4.9
|
47.3
|
1.0
|
HD2
|
A:LYS227
|
5.0
|
47.3
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 7rkh
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Magnesium Binding Sites List in 7rkh
Magnesium binding site 5 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg601
b:30.0
occ:1.00
|
HZ3
|
B:LYS227
|
2.9
|
47.3
|
1.0
|
O1B
|
A:UTP601
|
3.0
|
33.3
|
1.0
|
O2A
|
A:UTP601
|
3.1
|
33.3
|
1.0
|
O3B
|
A:UTP601
|
3.1
|
33.3
|
1.0
|
O3A
|
A:UTP601
|
3.1
|
33.3
|
1.0
|
PB
|
A:UTP601
|
3.3
|
33.3
|
1.0
|
HZ1
|
B:LYS227
|
3.7
|
47.3
|
1.0
|
PA
|
A:UTP601
|
3.7
|
33.3
|
1.0
|
NZ
|
B:LYS227
|
3.7
|
47.3
|
1.0
|
O3G
|
A:UTP601
|
3.7
|
33.3
|
1.0
|
HZ3
|
B:LYS191
|
3.8
|
41.5
|
1.0
|
PG
|
A:UTP601
|
3.9
|
33.3
|
1.0
|
HZ2
|
B:LYS227
|
4.0
|
47.3
|
1.0
|
HE2
|
A:HIS55
|
4.1
|
59.4
|
1.0
|
C5'
|
A:UTP601
|
4.2
|
33.3
|
1.0
|
HZ2
|
B:LYS191
|
4.2
|
41.5
|
1.0
|
O1G
|
A:UTP601
|
4.2
|
33.3
|
1.0
|
O5'
|
A:UTP601
|
4.2
|
33.3
|
1.0
|
NZ
|
B:LYS191
|
4.5
|
41.5
|
1.0
|
HG
|
A:SER12
|
4.6
|
42.8
|
1.0
|
NE2
|
A:HIS55
|
4.8
|
59.4
|
1.0
|
O2B
|
A:UTP601
|
4.8
|
33.3
|
1.0
|
HD2
|
A:HIS55
|
4.9
|
59.4
|
1.0
|
CE
|
B:LYS227
|
5.0
|
47.3
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 7rkh
Go back to
Magnesium Binding Sites List in 7rkh
Magnesium binding site 6 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg604
b:30.0
occ:1.00
|
OD2
|
B:ASP70
|
1.9
|
31.5
|
1.0
|
OD1
|
B:ASP70
|
2.4
|
31.5
|
1.0
|
CG
|
B:ASP70
|
2.4
|
31.5
|
1.0
|
O1B
|
B:ATP603
|
2.9
|
43.5
|
1.0
|
O3G
|
B:ATP603
|
3.0
|
43.5
|
1.0
|
HZ1
|
B:LYS16
|
3.1
|
26.8
|
1.0
|
OE2
|
B:GLU146
|
3.2
|
21.2
|
1.0
|
HA3
|
B:GLY17
|
3.3
|
37.3
|
1.0
|
HZ2
|
B:LYS16
|
3.3
|
26.8
|
1.0
|
H
|
B:GLY17
|
3.4
|
37.3
|
1.0
|
HZ3
|
B:LYS16
|
3.4
|
26.8
|
1.0
|
HZ3
|
B:LYS38
|
3.5
|
19.4
|
1.0
|
OE1
|
B:GLU146
|
3.5
|
21.2
|
1.0
|
HE3
|
B:LYS38
|
3.5
|
19.4
|
1.0
|
NZ
|
B:LYS16
|
3.6
|
26.8
|
1.0
|
CD
|
B:GLU146
|
3.7
|
21.2
|
1.0
|
O3B
|
B:ATP603
|
3.8
|
43.5
|
1.0
|
CB
|
B:ASP70
|
3.9
|
31.5
|
1.0
|
N
|
B:GLY17
|
3.9
|
37.3
|
1.0
|
HB2
|
B:LYS16
|
3.9
|
26.8
|
1.0
|
PB
|
B:ATP603
|
3.9
|
43.5
|
1.0
|
CA
|
B:GLY17
|
4.0
|
37.3
|
1.0
|
PG
|
B:ATP603
|
4.0
|
43.5
|
1.0
|
O2A
|
B:ATP603
|
4.0
|
43.5
|
1.0
|
HB3
|
B:ASP70
|
4.1
|
31.5
|
1.0
|
HA2
|
B:GLY17
|
4.1
|
37.3
|
1.0
|
NZ
|
B:LYS38
|
4.2
|
19.4
|
1.0
|
HD3
|
B:LYS38
|
4.2
|
19.4
|
1.0
|
CE
|
B:LYS38
|
4.3
|
19.4
|
1.0
|
HB2
|
B:ASP70
|
4.4
|
31.5
|
1.0
|
O4
|
B:UTP602
|
4.4
|
33.3
|
1.0
|
O1A
|
B:ATP603
|
4.5
|
43.5
|
1.0
|
HZ1
|
B:LYS38
|
4.5
|
19.4
|
1.0
|
PA
|
B:ATP603
|
4.5
|
43.5
|
1.0
|
O3A
|
B:ATP603
|
4.5
|
43.5
|
1.0
|
OD2
|
B:ASP68
|
4.6
|
39.0
|
1.0
|
HH
|
B:TYR74
|
4.6
|
28.7
|
1.0
|
HD13
|
B:LEU69
|
4.7
|
38.0
|
1.0
|
HA
|
B:ASP70
|
4.7
|
37.3
|
1.0
|
CD
|
B:LYS38
|
4.8
|
19.4
|
1.0
|
CA
|
B:ASP70
|
4.9
|
37.3
|
1.0
|
O2G
|
B:ATP603
|
4.9
|
43.5
|
1.0
|
C
|
B:LYS16
|
4.9
|
37.3
|
1.0
|
CB
|
B:LYS16
|
5.0
|
26.8
|
1.0
|
H
|
B:ASP70
|
5.0
|
37.3
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 7rkh
Go back to
Magnesium Binding Sites List in 7rkh
Magnesium binding site 7 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg601
b:30.0
occ:1.00
|
HZ3
|
C:LYS227
|
2.9
|
47.3
|
1.0
|
O2B
|
D:UTP601
|
3.0
|
33.3
|
1.0
|
O1A
|
D:UTP601
|
3.1
|
33.3
|
1.0
|
O3B
|
D:UTP601
|
3.1
|
33.3
|
1.0
|
O3A
|
D:UTP601
|
3.1
|
33.3
|
1.0
|
PB
|
D:UTP601
|
3.3
|
33.3
|
1.0
|
HZ1
|
C:LYS227
|
3.7
|
47.3
|
1.0
|
NZ
|
C:LYS227
|
3.7
|
47.3
|
1.0
|
PA
|
D:UTP601
|
3.7
|
33.3
|
1.0
|
O2G
|
D:UTP601
|
3.7
|
33.3
|
1.0
|
HZ3
|
C:LYS191
|
3.9
|
41.5
|
1.0
|
PG
|
D:UTP601
|
3.9
|
33.3
|
1.0
|
HZ2
|
C:LYS227
|
4.0
|
47.3
|
1.0
|
HE2
|
D:HIS55
|
4.1
|
59.4
|
1.0
|
C5'
|
D:UTP601
|
4.2
|
33.3
|
1.0
|
O1G
|
D:UTP601
|
4.2
|
33.3
|
1.0
|
O5'
|
D:UTP601
|
4.2
|
33.3
|
1.0
|
HZ2
|
C:LYS191
|
4.2
|
41.5
|
1.0
|
NZ
|
C:LYS191
|
4.6
|
41.5
|
1.0
|
HG
|
D:SER12
|
4.6
|
42.8
|
1.0
|
NE2
|
D:HIS55
|
4.8
|
59.4
|
1.0
|
O1B
|
D:UTP601
|
4.8
|
33.3
|
1.0
|
HD2
|
D:HIS55
|
4.9
|
59.4
|
1.0
|
CE
|
C:LYS227
|
4.9
|
47.3
|
1.0
|
HD2
|
C:LYS227
|
5.0
|
47.3
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 7rkh
Go back to
Magnesium Binding Sites List in 7rkh
Magnesium binding site 8 out
of 8 in the Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Yeast Ctp Synthase (URA8) Tetramer Bound to Atp/Utp at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg604
b:30.0
occ:1.00
|
OD2
|
C:ASP70
|
1.9
|
31.5
|
1.0
|
OD1
|
C:ASP70
|
2.4
|
31.5
|
1.0
|
CG
|
C:ASP70
|
2.4
|
31.5
|
1.0
|
O1B
|
C:ATP603
|
2.9
|
43.5
|
1.0
|
O3G
|
C:ATP603
|
3.0
|
43.5
|
1.0
|
HZ1
|
C:LYS16
|
3.1
|
26.8
|
1.0
|
OE2
|
C:GLU146
|
3.2
|
21.2
|
1.0
|
HA3
|
C:GLY17
|
3.3
|
37.3
|
1.0
|
HZ2
|
C:LYS16
|
3.4
|
26.8
|
1.0
|
H
|
C:GLY17
|
3.4
|
37.3
|
1.0
|
HZ3
|
C:LYS16
|
3.4
|
26.8
|
1.0
|
HZ3
|
C:LYS38
|
3.5
|
19.4
|
1.0
|
OE1
|
C:GLU146
|
3.5
|
21.2
|
1.0
|
HE3
|
C:LYS38
|
3.5
|
19.4
|
1.0
|
NZ
|
C:LYS16
|
3.6
|
26.8
|
1.0
|
CD
|
C:GLU146
|
3.7
|
21.2
|
1.0
|
O3B
|
C:ATP603
|
3.8
|
43.5
|
1.0
|
CB
|
C:ASP70
|
3.9
|
31.5
|
1.0
|
N
|
C:GLY17
|
3.9
|
37.3
|
1.0
|
HB2
|
C:LYS16
|
3.9
|
26.8
|
1.0
|
PB
|
C:ATP603
|
3.9
|
43.5
|
1.0
|
CA
|
C:GLY17
|
4.0
|
37.3
|
1.0
|
PG
|
C:ATP603
|
4.0
|
43.5
|
1.0
|
O2A
|
C:ATP603
|
4.0
|
43.5
|
1.0
|
HB3
|
C:ASP70
|
4.1
|
31.5
|
1.0
|
HA2
|
C:GLY17
|
4.1
|
37.3
|
1.0
|
NZ
|
C:LYS38
|
4.2
|
19.4
|
1.0
|
HD3
|
C:LYS38
|
4.2
|
19.4
|
1.0
|
CE
|
C:LYS38
|
4.3
|
19.4
|
1.0
|
HB2
|
C:ASP70
|
4.4
|
31.5
|
1.0
|
O4
|
C:UTP602
|
4.4
|
33.3
|
1.0
|
O1A
|
C:ATP603
|
4.5
|
43.5
|
1.0
|
HZ1
|
C:LYS38
|
4.5
|
19.4
|
1.0
|
PA
|
C:ATP603
|
4.5
|
43.5
|
1.0
|
O3A
|
C:ATP603
|
4.6
|
43.5
|
1.0
|
OD2
|
C:ASP68
|
4.6
|
39.0
|
1.0
|
HH
|
C:TYR74
|
4.6
|
28.7
|
1.0
|
HD13
|
C:LEU69
|
4.7
|
38.0
|
1.0
|
HA
|
C:ASP70
|
4.7
|
37.3
|
1.0
|
CD
|
C:LYS38
|
4.8
|
19.4
|
1.0
|
CA
|
C:ASP70
|
4.9
|
37.3
|
1.0
|
O2G
|
C:ATP603
|
4.9
|
43.5
|
1.0
|
C
|
C:LYS16
|
4.9
|
37.3
|
1.0
|
CB
|
C:LYS16
|
5.0
|
26.8
|
1.0
|
H
|
C:ASP70
|
5.0
|
37.3
|
1.0
|
|
Reference:
J.M.Hansen,
A.Horowitz,
E.M.Lynch,
D.P.Farrell,
J.Quispe,
F.Dimaio,
J.M.Kollman.
Cryo-Em Structures of Ctp Synthase Filaments Reveal Mechanism of pH-Sensitive Assembly During Budding Yeast Starvation. Elife V. 10 2021.
ISSN: ESSN 2050-084X
PubMed: 34734801
DOI: 10.7554/ELIFE.73368
Page generated: Thu Oct 3 07:59:00 2024
|