Magnesium in PDB 8io9: Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
Magnesium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
(pdb code 8io9). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the
Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly, PDB code: 8io9:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 1 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg903
b:111.7
occ:1.00
|
O2A
|
A:TPP902
|
2.0
|
113.5
|
1.0
|
|
O
|
A:TYR213
|
2.0
|
117.9
|
1.0
|
|
OD1
|
A:ASN211
|
2.0
|
111.7
|
1.0
|
|
O2B
|
A:TPP902
|
2.1
|
113.5
|
1.0
|
|
ND2
|
A:ASN211
|
2.5
|
111.7
|
1.0
|
|
CG
|
A:ASN211
|
2.6
|
111.7
|
1.0
|
|
OD1
|
A:ASP178
|
2.7
|
109.9
|
1.0
|
|
PA
|
A:TPP902
|
3.2
|
113.5
|
1.0
|
|
C
|
A:TYR213
|
3.2
|
117.9
|
1.0
|
|
PB
|
A:TPP902
|
3.3
|
113.5
|
1.0
|
|
O3A
|
A:TPP902
|
3.4
|
113.5
|
1.0
|
|
CG
|
A:ASP178
|
3.4
|
109.9
|
1.0
|
|
OD2
|
A:ASP178
|
3.5
|
109.9
|
1.0
|
|
NZ
|
A:LYS293
|
3.7
|
115.1
|
1.0
|
|
N
|
A:TYR213
|
4.0
|
117.9
|
1.0
|
|
CE
|
A:LYS293
|
4.1
|
115.1
|
1.0
|
|
O1B
|
A:TPP902
|
4.1
|
113.5
|
1.0
|
|
CB
|
A:ASN211
|
4.1
|
111.7
|
1.0
|
|
O1A
|
A:TPP902
|
4.1
|
113.5
|
1.0
|
|
N
|
A:LYS214
|
4.2
|
117.4
|
1.0
|
|
CA
|
A:TYR213
|
4.2
|
117.9
|
1.0
|
|
O7
|
A:TPP902
|
4.3
|
113.5
|
1.0
|
|
CA
|
A:LYS214
|
4.3
|
117.4
|
1.0
|
|
O3B
|
A:TPP902
|
4.4
|
113.5
|
1.0
|
|
CG2
|
A:THR219
|
4.5
|
114.5
|
1.0
|
|
N
|
A:GLY179
|
4.5
|
108.0
|
1.0
|
|
CD
|
A:LYS293
|
4.6
|
115.1
|
1.0
|
|
N
|
A:ASP178
|
4.8
|
109.9
|
1.0
|
|
N
|
A:ASN211
|
4.8
|
111.7
|
1.0
|
|
CB
|
A:ASP178
|
4.8
|
109.9
|
1.0
|
|
CA
|
A:ASN211
|
4.9
|
111.7
|
1.0
|
|
N
|
A:GLY212
|
4.9
|
114.0
|
1.0
|
|
O
|
A:HIS209
|
5.0
|
108.6
|
1.0
|
|
C
|
A:ASN211
|
5.0
|
111.7
|
1.0
|
|
Magnesium binding site 2 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 2 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg903
b:114.6
occ:1.00
|
O1A
|
B:TPP902
|
2.0
|
115.2
|
1.0
|
|
O
|
B:TYR213
|
2.0
|
117.7
|
1.0
|
|
OD1
|
B:ASN211
|
2.0
|
114.3
|
1.0
|
|
O1B
|
B:TPP902
|
2.1
|
115.2
|
1.0
|
|
ND2
|
B:ASN211
|
2.6
|
114.3
|
1.0
|
|
CG
|
B:ASN211
|
2.6
|
114.3
|
1.0
|
|
OD1
|
B:ASP178
|
2.7
|
111.6
|
1.0
|
|
PA
|
B:TPP902
|
3.2
|
115.2
|
1.0
|
|
C
|
B:TYR213
|
3.2
|
117.7
|
1.0
|
|
PB
|
B:TPP902
|
3.3
|
115.2
|
1.0
|
|
O3A
|
B:TPP902
|
3.4
|
115.2
|
1.0
|
|
CG
|
B:ASP178
|
3.6
|
111.6
|
1.0
|
|
NZ
|
B:LYS293
|
3.7
|
116.0
|
1.0
|
|
OD2
|
B:ASP178
|
3.8
|
111.6
|
1.0
|
|
N
|
B:TYR213
|
4.0
|
117.7
|
1.0
|
|
O2B
|
B:TPP902
|
4.1
|
115.2
|
1.0
|
|
CB
|
B:ASN211
|
4.1
|
114.3
|
1.0
|
|
CE
|
B:LYS293
|
4.1
|
116.0
|
1.0
|
|
N
|
B:LYS214
|
4.2
|
117.5
|
1.0
|
|
CA
|
B:TYR213
|
4.2
|
117.7
|
1.0
|
|
O7
|
B:TPP902
|
4.2
|
115.2
|
1.0
|
|
O2A
|
B:TPP902
|
4.3
|
115.2
|
1.0
|
|
CA
|
B:LYS214
|
4.3
|
117.5
|
1.0
|
|
CG2
|
B:THR219
|
4.4
|
117.3
|
1.0
|
|
N
|
B:GLY179
|
4.4
|
109.0
|
1.0
|
|
O3B
|
B:TPP902
|
4.4
|
115.2
|
1.0
|
|
CD
|
B:LYS293
|
4.6
|
116.0
|
1.0
|
|
N
|
B:ASP178
|
4.7
|
111.6
|
1.0
|
|
N
|
B:ASN211
|
4.8
|
114.3
|
1.0
|
|
N
|
B:GLY212
|
4.8
|
114.7
|
1.0
|
|
CA
|
B:ASN211
|
4.8
|
114.3
|
1.0
|
|
C
|
B:ASN211
|
4.9
|
114.3
|
1.0
|
|
CB
|
B:ASP178
|
4.9
|
111.6
|
1.0
|
|
O
|
B:HIS209
|
4.9
|
110.4
|
1.0
|
|
CB
|
B:TYR213
|
5.0
|
117.7
|
1.0
|
|
Magnesium binding site 3 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 3 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg903
b:110.2
occ:1.00
|
O2A
|
C:TPP902
|
2.0
|
113.8
|
1.0
|
|
O
|
C:TYR213
|
2.0
|
117.7
|
1.0
|
|
OD1
|
C:ASN211
|
2.0
|
112.4
|
1.0
|
|
O2B
|
C:TPP902
|
2.1
|
113.8
|
1.0
|
|
ND2
|
C:ASN211
|
2.6
|
112.4
|
1.0
|
|
CG
|
C:ASN211
|
2.6
|
112.4
|
1.0
|
|
OD1
|
C:ASP178
|
2.7
|
110.0
|
1.0
|
|
PA
|
C:TPP902
|
3.2
|
113.8
|
1.0
|
|
C
|
C:TYR213
|
3.2
|
117.7
|
1.0
|
|
PB
|
C:TPP902
|
3.3
|
113.8
|
1.0
|
|
O3A
|
C:TPP902
|
3.5
|
113.8
|
1.0
|
|
CG
|
C:ASP178
|
3.7
|
110.0
|
1.0
|
|
NZ
|
C:LYS293
|
3.7
|
118.3
|
1.0
|
|
OD2
|
C:ASP178
|
3.9
|
110.0
|
1.0
|
|
N
|
C:TYR213
|
4.0
|
117.7
|
1.0
|
|
CE
|
C:LYS293
|
4.1
|
118.3
|
1.0
|
|
CB
|
C:ASN211
|
4.1
|
112.4
|
1.0
|
|
O1B
|
C:TPP902
|
4.1
|
113.8
|
1.0
|
|
N
|
C:LYS214
|
4.1
|
116.5
|
1.0
|
|
CA
|
C:TYR213
|
4.2
|
117.7
|
1.0
|
|
O7
|
C:TPP902
|
4.2
|
113.8
|
1.0
|
|
O1A
|
C:TPP902
|
4.2
|
113.8
|
1.0
|
|
CA
|
C:LYS214
|
4.3
|
116.5
|
1.0
|
|
CG2
|
C:THR219
|
4.4
|
113.6
|
1.0
|
|
O3B
|
C:TPP902
|
4.4
|
113.8
|
1.0
|
|
N
|
C:GLY179
|
4.5
|
106.9
|
1.0
|
|
CD
|
C:LYS293
|
4.6
|
118.3
|
1.0
|
|
N
|
C:ASP178
|
4.8
|
110.0
|
1.0
|
|
N
|
C:ASN211
|
4.8
|
112.4
|
1.0
|
|
N
|
C:GLY212
|
4.8
|
113.7
|
1.0
|
|
CA
|
C:ASN211
|
4.9
|
112.4
|
1.0
|
|
C
|
C:ASN211
|
4.9
|
112.4
|
1.0
|
|
O
|
C:HIS209
|
5.0
|
110.1
|
1.0
|
|
CB
|
C:TYR213
|
5.0
|
117.7
|
1.0
|
|
Magnesium binding site 4 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 4 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg903
b:109.7
occ:1.00
|
O1A
|
D:TPP902
|
2.0
|
113.5
|
1.0
|
|
O
|
D:TYR213
|
2.0
|
117.0
|
1.0
|
|
OD1
|
D:ASN211
|
2.0
|
113.0
|
1.0
|
|
O1B
|
D:TPP902
|
2.1
|
113.5
|
1.0
|
|
CG
|
D:ASN211
|
2.7
|
113.0
|
1.0
|
|
ND2
|
D:ASN211
|
2.7
|
113.0
|
1.0
|
|
OD1
|
D:ASP178
|
2.7
|
110.3
|
1.0
|
|
PA
|
D:TPP902
|
3.2
|
113.5
|
1.0
|
|
C
|
D:TYR213
|
3.2
|
117.0
|
1.0
|
|
PB
|
D:TPP902
|
3.3
|
113.5
|
1.0
|
|
O3A
|
D:TPP902
|
3.4
|
113.5
|
1.0
|
|
CG
|
D:ASP178
|
3.6
|
110.3
|
1.0
|
|
NZ
|
D:LYS293
|
3.7
|
118.3
|
1.0
|
|
OD2
|
D:ASP178
|
3.8
|
110.3
|
1.0
|
|
N
|
D:TYR213
|
4.0
|
117.0
|
1.0
|
|
O2B
|
D:TPP902
|
4.1
|
113.5
|
1.0
|
|
CE
|
D:LYS293
|
4.1
|
118.3
|
1.0
|
|
CB
|
D:ASN211
|
4.1
|
113.0
|
1.0
|
|
N
|
D:LYS214
|
4.1
|
116.8
|
1.0
|
|
CA
|
D:TYR213
|
4.2
|
117.0
|
1.0
|
|
O7
|
D:TPP902
|
4.2
|
113.5
|
1.0
|
|
O2A
|
D:TPP902
|
4.3
|
113.5
|
1.0
|
|
CA
|
D:LYS214
|
4.3
|
116.8
|
1.0
|
|
CG2
|
D:THR219
|
4.4
|
114.2
|
1.0
|
|
O3B
|
D:TPP902
|
4.4
|
113.5
|
1.0
|
|
N
|
D:GLY179
|
4.4
|
107.2
|
1.0
|
|
CD
|
D:LYS293
|
4.6
|
118.3
|
1.0
|
|
N
|
D:ASP178
|
4.7
|
110.3
|
1.0
|
|
N
|
D:ASN211
|
4.8
|
113.0
|
1.0
|
|
N
|
D:GLY212
|
4.8
|
113.5
|
1.0
|
|
CA
|
D:ASN211
|
4.9
|
113.0
|
1.0
|
|
C
|
D:ASN211
|
4.9
|
113.0
|
1.0
|
|
O
|
D:HIS209
|
4.9
|
109.6
|
1.0
|
|
CB
|
D:ASP178
|
4.9
|
110.3
|
1.0
|
|
CB
|
D:TYR213
|
5.0
|
117.0
|
1.0
|
|
Magnesium binding site 5 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 5 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg903
b:114.6
occ:1.00
|
O2A
|
E:TPP902
|
2.0
|
115.3
|
1.0
|
|
O
|
E:TYR213
|
2.0
|
118.2
|
1.0
|
|
OD1
|
E:ASN211
|
2.0
|
113.8
|
1.0
|
|
O2B
|
E:TPP902
|
2.1
|
115.3
|
1.0
|
|
ND2
|
E:ASN211
|
2.6
|
113.8
|
1.0
|
|
CG
|
E:ASN211
|
2.6
|
113.8
|
1.0
|
|
OD1
|
E:ASP178
|
2.7
|
111.0
|
1.0
|
|
PA
|
E:TPP902
|
3.2
|
115.3
|
1.0
|
|
C
|
E:TYR213
|
3.2
|
118.2
|
1.0
|
|
PB
|
E:TPP902
|
3.3
|
115.3
|
1.0
|
|
O3A
|
E:TPP902
|
3.4
|
115.3
|
1.0
|
|
CG
|
E:ASP178
|
3.7
|
111.0
|
1.0
|
|
NZ
|
E:LYS293
|
3.7
|
116.2
|
1.0
|
|
OD2
|
E:ASP178
|
3.9
|
111.0
|
1.0
|
|
N
|
E:TYR213
|
4.0
|
118.2
|
1.0
|
|
O1B
|
E:TPP902
|
4.1
|
115.3
|
1.0
|
|
CB
|
E:ASN211
|
4.1
|
113.8
|
1.0
|
|
N
|
E:LYS214
|
4.1
|
117.9
|
1.0
|
|
CE
|
E:LYS293
|
4.2
|
116.2
|
1.0
|
|
CA
|
E:TYR213
|
4.2
|
118.2
|
1.0
|
|
O1A
|
E:TPP902
|
4.2
|
115.3
|
1.0
|
|
O7
|
E:TPP902
|
4.3
|
115.3
|
1.0
|
|
CA
|
E:LYS214
|
4.3
|
117.9
|
1.0
|
|
CG2
|
E:THR219
|
4.4
|
116.6
|
1.0
|
|
N
|
E:GLY179
|
4.5
|
108.9
|
1.0
|
|
O3B
|
E:TPP902
|
4.5
|
115.3
|
1.0
|
|
CD
|
E:LYS293
|
4.6
|
116.2
|
1.0
|
|
N
|
E:ASP178
|
4.8
|
111.0
|
1.0
|
|
N
|
E:ASN211
|
4.8
|
113.8
|
1.0
|
|
N
|
E:GLY212
|
4.8
|
114.9
|
1.0
|
|
CA
|
E:ASN211
|
4.8
|
113.8
|
1.0
|
|
C
|
E:ASN211
|
4.9
|
113.8
|
1.0
|
|
O
|
E:HIS209
|
5.0
|
110.6
|
1.0
|
|
CB
|
E:TYR213
|
5.0
|
118.2
|
1.0
|
|
Magnesium binding site 6 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 6 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg903
b:111.8
occ:1.00
|
O1A
|
F:TPP902
|
2.0
|
113.7
|
1.0
|
|
O
|
F:TYR213
|
2.0
|
117.8
|
1.0
|
|
OD1
|
F:ASN211
|
2.0
|
112.8
|
1.0
|
|
O1B
|
F:TPP902
|
2.1
|
113.7
|
1.0
|
|
ND2
|
F:ASN211
|
2.6
|
112.8
|
1.0
|
|
CG
|
F:ASN211
|
2.6
|
112.8
|
1.0
|
|
OD1
|
F:ASP178
|
2.8
|
110.8
|
1.0
|
|
PA
|
F:TPP902
|
3.2
|
113.7
|
1.0
|
|
C
|
F:TYR213
|
3.2
|
117.8
|
1.0
|
|
PB
|
F:TPP902
|
3.3
|
113.7
|
1.0
|
|
O3A
|
F:TPP902
|
3.4
|
113.7
|
1.0
|
|
NZ
|
F:LYS293
|
3.7
|
116.2
|
1.0
|
|
CG
|
F:ASP178
|
3.7
|
110.8
|
1.0
|
|
OD2
|
F:ASP178
|
3.9
|
110.8
|
1.0
|
|
N
|
F:TYR213
|
4.0
|
117.8
|
1.0
|
|
O2B
|
F:TPP902
|
4.1
|
113.7
|
1.0
|
|
CB
|
F:ASN211
|
4.1
|
112.8
|
1.0
|
|
CE
|
F:LYS293
|
4.1
|
116.2
|
1.0
|
|
O2A
|
F:TPP902
|
4.1
|
113.7
|
1.0
|
|
N
|
F:LYS214
|
4.2
|
117.9
|
1.0
|
|
CA
|
F:TYR213
|
4.2
|
117.8
|
1.0
|
|
O7
|
F:TPP902
|
4.3
|
113.7
|
1.0
|
|
CA
|
F:LYS214
|
4.3
|
117.9
|
1.0
|
|
O3B
|
F:TPP902
|
4.5
|
113.7
|
1.0
|
|
CG2
|
F:THR219
|
4.5
|
115.3
|
1.0
|
|
N
|
F:GLY179
|
4.5
|
108.2
|
1.0
|
|
CD
|
F:LYS293
|
4.6
|
116.2
|
1.0
|
|
N
|
F:ASN211
|
4.8
|
112.8
|
1.0
|
|
N
|
F:ASP178
|
4.8
|
110.8
|
1.0
|
|
N
|
F:GLY212
|
4.8
|
114.3
|
1.0
|
|
CA
|
F:ASN211
|
4.8
|
112.8
|
1.0
|
|
O
|
F:HIS209
|
4.9
|
109.4
|
1.0
|
|
C
|
F:ASN211
|
4.9
|
112.8
|
1.0
|
|
CB
|
F:TYR213
|
5.0
|
117.8
|
1.0
|
|
Magnesium binding site 7 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 7 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg903
b:111.6
occ:1.00
|
O2A
|
G:TPP902
|
2.0
|
113.1
|
1.0
|
|
O
|
G:TYR213
|
2.0
|
117.7
|
1.0
|
|
OD1
|
G:ASN211
|
2.0
|
111.7
|
1.0
|
|
O2B
|
G:TPP902
|
2.1
|
113.1
|
1.0
|
|
ND2
|
G:ASN211
|
2.5
|
111.7
|
1.0
|
|
CG
|
G:ASN211
|
2.6
|
111.7
|
1.0
|
|
OD1
|
G:ASP178
|
2.8
|
109.8
|
1.0
|
|
PA
|
G:TPP902
|
3.2
|
113.1
|
1.0
|
|
C
|
G:TYR213
|
3.2
|
117.7
|
1.0
|
|
PB
|
G:TPP902
|
3.3
|
113.1
|
1.0
|
|
O3A
|
G:TPP902
|
3.4
|
113.1
|
1.0
|
|
NZ
|
G:LYS293
|
3.7
|
115.6
|
1.0
|
|
CG
|
G:ASP178
|
3.7
|
109.8
|
1.0
|
|
OD2
|
G:ASP178
|
3.9
|
109.8
|
1.0
|
|
N
|
G:TYR213
|
4.0
|
117.7
|
1.0
|
|
CB
|
G:ASN211
|
4.1
|
111.7
|
1.0
|
|
O1B
|
G:TPP902
|
4.1
|
113.1
|
1.0
|
|
CE
|
G:LYS293
|
4.1
|
115.6
|
1.0
|
|
N
|
G:LYS214
|
4.1
|
117.4
|
1.0
|
|
O1A
|
G:TPP902
|
4.2
|
113.1
|
1.0
|
|
CA
|
G:TYR213
|
4.2
|
117.7
|
1.0
|
|
O7
|
G:TPP902
|
4.3
|
113.1
|
1.0
|
|
CA
|
G:LYS214
|
4.3
|
117.4
|
1.0
|
|
O3B
|
G:TPP902
|
4.5
|
113.1
|
1.0
|
|
CG2
|
G:THR219
|
4.5
|
115.0
|
1.0
|
|
N
|
G:GLY179
|
4.5
|
107.7
|
1.0
|
|
CD
|
G:LYS293
|
4.6
|
115.6
|
1.0
|
|
N
|
G:ASP178
|
4.8
|
109.8
|
1.0
|
|
N
|
G:ASN211
|
4.8
|
111.7
|
1.0
|
|
CA
|
G:ASN211
|
4.9
|
111.7
|
1.0
|
|
N
|
G:GLY212
|
4.9
|
113.5
|
1.0
|
|
O
|
G:HIS209
|
5.0
|
108.7
|
1.0
|
|
C
|
G:ASN211
|
5.0
|
111.7
|
1.0
|
|
Magnesium binding site 8 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 8 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg903
b:114.6
occ:1.00
|
O1A
|
H:TPP902
|
2.0
|
115.0
|
1.0
|
|
O
|
H:TYR213
|
2.0
|
117.4
|
1.0
|
|
OD1
|
H:ASN211
|
2.0
|
114.1
|
1.0
|
|
O1B
|
H:TPP902
|
2.1
|
115.0
|
1.0
|
|
ND2
|
H:ASN211
|
2.6
|
114.1
|
1.0
|
|
CG
|
H:ASN211
|
2.6
|
114.1
|
1.0
|
|
OD1
|
H:ASP178
|
2.7
|
111.7
|
1.0
|
|
PA
|
H:TPP902
|
3.2
|
115.0
|
1.0
|
|
C
|
H:TYR213
|
3.2
|
117.4
|
1.0
|
|
PB
|
H:TPP902
|
3.3
|
115.0
|
1.0
|
|
O3A
|
H:TPP902
|
3.4
|
115.0
|
1.0
|
|
CG
|
H:ASP178
|
3.6
|
111.7
|
1.0
|
|
NZ
|
H:LYS293
|
3.7
|
116.5
|
1.0
|
|
OD2
|
H:ASP178
|
3.9
|
111.7
|
1.0
|
|
N
|
H:TYR213
|
4.0
|
117.4
|
1.0
|
|
O2B
|
H:TPP902
|
4.1
|
115.0
|
1.0
|
|
CB
|
H:ASN211
|
4.1
|
114.1
|
1.0
|
|
N
|
H:LYS214
|
4.1
|
117.8
|
1.0
|
|
CE
|
H:LYS293
|
4.2
|
116.5
|
1.0
|
|
CA
|
H:TYR213
|
4.2
|
117.4
|
1.0
|
|
O7
|
H:TPP902
|
4.2
|
115.0
|
1.0
|
|
O2A
|
H:TPP902
|
4.3
|
115.0
|
1.0
|
|
CA
|
H:LYS214
|
4.3
|
117.8
|
1.0
|
|
CG2
|
H:THR219
|
4.4
|
117.2
|
1.0
|
|
N
|
H:GLY179
|
4.4
|
109.7
|
1.0
|
|
O3B
|
H:TPP902
|
4.4
|
115.0
|
1.0
|
|
CD
|
H:LYS293
|
4.6
|
116.5
|
1.0
|
|
N
|
H:ASP178
|
4.7
|
111.7
|
1.0
|
|
N
|
H:ASN211
|
4.8
|
114.1
|
1.0
|
|
N
|
H:GLY212
|
4.8
|
114.5
|
1.0
|
|
CA
|
H:ASN211
|
4.8
|
114.1
|
1.0
|
|
C
|
H:ASN211
|
4.9
|
114.1
|
1.0
|
|
CB
|
H:ASP178
|
4.9
|
111.7
|
1.0
|
|
O
|
H:HIS209
|
5.0
|
110.3
|
1.0
|
|
CB
|
H:TYR213
|
5.0
|
117.4
|
1.0
|
|
Magnesium binding site 9 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 9 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mg903
b:109.9
occ:1.00
|
O2A
|
I:TPP902
|
2.0
|
113.3
|
1.0
|
|
O
|
I:TYR213
|
2.0
|
117.5
|
1.0
|
|
OD1
|
I:ASN211
|
2.0
|
112.5
|
1.0
|
|
O2B
|
I:TPP902
|
2.1
|
113.3
|
1.0
|
|
ND2
|
I:ASN211
|
2.6
|
112.5
|
1.0
|
|
CG
|
I:ASN211
|
2.6
|
112.5
|
1.0
|
|
OD1
|
I:ASP178
|
2.7
|
109.7
|
1.0
|
|
PA
|
I:TPP902
|
3.2
|
113.3
|
1.0
|
|
C
|
I:TYR213
|
3.2
|
117.5
|
1.0
|
|
PB
|
I:TPP902
|
3.3
|
113.3
|
1.0
|
|
O3A
|
I:TPP902
|
3.4
|
113.3
|
1.0
|
|
CG
|
I:ASP178
|
3.7
|
109.7
|
1.0
|
|
NZ
|
I:LYS293
|
3.7
|
117.8
|
1.0
|
|
OD2
|
I:ASP178
|
3.9
|
109.7
|
1.0
|
|
N
|
I:TYR213
|
4.0
|
117.5
|
1.0
|
|
O1B
|
I:TPP902
|
4.1
|
113.3
|
1.0
|
|
CB
|
I:ASN211
|
4.1
|
112.5
|
1.0
|
|
N
|
I:LYS214
|
4.1
|
116.3
|
1.0
|
|
CE
|
I:LYS293
|
4.1
|
117.8
|
1.0
|
|
O1A
|
I:TPP902
|
4.2
|
113.3
|
1.0
|
|
CA
|
I:TYR213
|
4.2
|
117.5
|
1.0
|
|
O7
|
I:TPP902
|
4.3
|
113.3
|
1.0
|
|
CA
|
I:LYS214
|
4.3
|
116.3
|
1.0
|
|
CG2
|
I:THR219
|
4.4
|
113.7
|
1.0
|
|
O3B
|
I:TPP902
|
4.4
|
113.3
|
1.0
|
|
N
|
I:GLY179
|
4.4
|
106.3
|
1.0
|
|
CD
|
I:LYS293
|
4.6
|
117.8
|
1.0
|
|
N
|
I:ASP178
|
4.8
|
109.7
|
1.0
|
|
N
|
I:ASN211
|
4.8
|
112.5
|
1.0
|
|
N
|
I:GLY212
|
4.8
|
113.9
|
1.0
|
|
CA
|
I:ASN211
|
4.9
|
112.5
|
1.0
|
|
C
|
I:ASN211
|
5.0
|
112.5
|
1.0
|
|
O
|
I:HIS209
|
5.0
|
109.5
|
1.0
|
|
CB
|
I:TYR213
|
5.0
|
117.5
|
1.0
|
|
Magnesium binding site 10 out
of 12 in 8io9
Go back to
Magnesium Binding Sites List in 8io9
Magnesium binding site 10 out
of 12 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnp in Dodecameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Mg903
b:109.9
occ:1.00
|
O1A
|
J:TPP902
|
2.0
|
113.2
|
1.0
|
|
O
|
J:TYR213
|
2.0
|
116.9
|
1.0
|
|
OD1
|
J:ASN211
|
2.0
|
112.9
|
1.0
|
|
O1B
|
J:TPP902
|
2.1
|
113.2
|
1.0
|
|
CG
|
J:ASN211
|
2.7
|
112.9
|
1.0
|
|
ND2
|
J:ASN211
|
2.7
|
112.9
|
1.0
|
|
OD1
|
J:ASP178
|
2.7
|
109.6
|
1.0
|
|
PA
|
J:TPP902
|
3.2
|
113.2
|
1.0
|
|
C
|
J:TYR213
|
3.2
|
116.9
|
1.0
|
|
PB
|
J:TPP902
|
3.3
|
113.2
|
1.0
|
|
O3A
|
J:TPP902
|
3.4
|
113.2
|
1.0
|
|
CG
|
J:ASP178
|
3.7
|
109.6
|
1.0
|
|
NZ
|
J:LYS293
|
3.7
|
118.4
|
1.0
|
|
OD2
|
J:ASP178
|
3.9
|
109.6
|
1.0
|
|
N
|
J:TYR213
|
4.0
|
116.9
|
1.0
|
|
O2B
|
J:TPP902
|
4.1
|
113.2
|
1.0
|
|
O2A
|
J:TPP902
|
4.1
|
113.2
|
1.0
|
|
CB
|
J:ASN211
|
4.1
|
112.9
|
1.0
|
|
N
|
J:LYS214
|
4.2
|
116.6
|
1.0
|
|
CE
|
J:LYS293
|
4.2
|
118.4
|
1.0
|
|
CA
|
J:TYR213
|
4.2
|
116.9
|
1.0
|
|
O7
|
J:TPP902
|
4.3
|
113.2
|
1.0
|
|
CA
|
J:LYS214
|
4.3
|
116.6
|
1.0
|
|
CG2
|
J:THR219
|
4.4
|
114.5
|
1.0
|
|
O3B
|
J:TPP902
|
4.5
|
113.2
|
1.0
|
|
N
|
J:GLY179
|
4.5
|
106.4
|
1.0
|
|
CD
|
J:LYS293
|
4.6
|
118.4
|
1.0
|
|
N
|
J:ASP178
|
4.8
|
109.6
|
1.0
|
|
N
|
J:ASN211
|
4.8
|
112.9
|
1.0
|
|
N
|
J:GLY212
|
4.8
|
113.5
|
1.0
|
|
CA
|
J:ASN211
|
4.8
|
112.9
|
1.0
|
|
C
|
J:ASN211
|
4.9
|
112.9
|
1.0
|
|
O
|
J:HIS209
|
5.0
|
109.8
|
1.0
|
|
CB
|
J:TYR213
|
5.0
|
116.9
|
1.0
|
|
Reference:
C.-W.Chang,
M.-D.Tsai.
An Atp-Sensitive Phosphoketolase Regulates Carbon Fixation in Cyanobacteria. Nat Metab 2023.
ISSN: ISSN 2522-5812
DOI: 10.1038/S42255-023-00831-W
Page generated: Fri Jul 28 01:40:30 2023
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