Magnesium in PDB 8io6: Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric Assembly
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric Assembly
(pdb code 8io6). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric Assembly, PDB code: 8io6:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 1 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg901
b:23.4
occ:1.00
|
O2B
|
A:TPP900
|
1.9
|
26.7
|
1.0
|
|
OD1
|
A:ASN215
|
2.0
|
20.3
|
1.0
|
|
OD1
|
A:ASP182
|
2.0
|
21.8
|
1.0
|
|
O
|
A:TYR217
|
2.2
|
23.1
|
1.0
|
|
O2A
|
A:TPP900
|
2.5
|
26.7
|
1.0
|
|
CG
|
A:ASP182
|
2.9
|
21.8
|
1.0
|
|
CG
|
A:ASN215
|
3.1
|
20.3
|
1.0
|
|
PB
|
A:TPP900
|
3.2
|
26.7
|
1.0
|
|
OD2
|
A:ASP182
|
3.2
|
21.8
|
1.0
|
|
C
|
A:TYR217
|
3.3
|
23.1
|
1.0
|
|
ND2
|
A:ASN215
|
3.6
|
20.3
|
1.0
|
|
N
|
A:TYR217
|
3.6
|
23.1
|
1.0
|
|
O3A
|
A:TPP900
|
3.7
|
26.7
|
1.0
|
|
PA
|
A:TPP900
|
3.7
|
26.7
|
1.0
|
|
O1B
|
A:TPP900
|
4.0
|
26.7
|
1.0
|
|
CA
|
A:TYR217
|
4.1
|
23.1
|
1.0
|
|
NZ
|
A:LYS300
|
4.1
|
22.1
|
1.0
|
|
N
|
A:GLY183
|
4.2
|
25.2
|
1.0
|
|
N
|
A:GLY216
|
4.2
|
21.7
|
1.0
|
|
N
|
A:ASP182
|
4.3
|
21.8
|
1.0
|
|
CG2
|
A:THR223
|
4.3
|
23.2
|
1.0
|
|
N
|
A:ASN215
|
4.3
|
20.3
|
1.0
|
|
N
|
A:LYS218
|
4.3
|
26.1
|
1.0
|
|
CB
|
A:ASP182
|
4.3
|
21.8
|
1.0
|
|
CB
|
A:ASN215
|
4.3
|
20.3
|
1.0
|
|
O3B
|
A:TPP900
|
4.4
|
26.7
|
1.0
|
|
O
|
A:HIS213
|
4.4
|
19.5
|
1.0
|
|
C
|
A:ASN215
|
4.4
|
20.3
|
1.0
|
|
CA
|
A:ASN215
|
4.6
|
20.3
|
1.0
|
|
C
|
A:GLY216
|
4.6
|
21.7
|
1.0
|
|
O1A
|
A:TPP900
|
4.7
|
26.7
|
1.0
|
|
CA
|
A:ASP182
|
4.7
|
21.8
|
1.0
|
|
O7
|
A:TPP900
|
4.8
|
26.7
|
1.0
|
|
CA
|
A:LYS218
|
4.8
|
26.1
|
1.0
|
|
CD
|
A:LYS300
|
4.8
|
22.1
|
1.0
|
|
C
|
A:ASP182
|
4.9
|
21.8
|
1.0
|
|
CE
|
A:LYS300
|
4.9
|
22.1
|
1.0
|
|
CA
|
A:GLY216
|
5.0
|
21.7
|
1.0
|
|
CB
|
A:TYR217
|
5.0
|
23.1
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 2 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg901
b:23.1
occ:1.00
|
O1B
|
B:TPP900
|
1.9
|
26.4
|
1.0
|
|
OD1
|
B:ASN215
|
2.0
|
20.2
|
1.0
|
|
OD1
|
B:ASP182
|
2.0
|
21.7
|
1.0
|
|
O
|
B:TYR217
|
2.2
|
23.0
|
1.0
|
|
O1A
|
B:TPP900
|
2.5
|
26.4
|
1.0
|
|
CG
|
B:ASP182
|
2.9
|
21.7
|
1.0
|
|
CG
|
B:ASN215
|
3.1
|
20.2
|
1.0
|
|
PB
|
B:TPP900
|
3.2
|
26.4
|
1.0
|
|
OD2
|
B:ASP182
|
3.2
|
21.7
|
1.0
|
|
C
|
B:TYR217
|
3.3
|
23.0
|
1.0
|
|
ND2
|
B:ASN215
|
3.6
|
20.2
|
1.0
|
|
N
|
B:TYR217
|
3.6
|
23.0
|
1.0
|
|
O3A
|
B:TPP900
|
3.7
|
26.4
|
1.0
|
|
PA
|
B:TPP900
|
3.7
|
26.4
|
1.0
|
|
O2B
|
B:TPP900
|
4.0
|
26.4
|
1.0
|
|
CA
|
B:TYR217
|
4.1
|
23.0
|
1.0
|
|
NZ
|
B:LYS300
|
4.1
|
21.9
|
1.0
|
|
N
|
B:GLY183
|
4.2
|
25.0
|
1.0
|
|
N
|
B:GLY216
|
4.2
|
21.5
|
1.0
|
|
N
|
B:ASP182
|
4.3
|
21.7
|
1.0
|
|
CG2
|
B:THR223
|
4.3
|
23.1
|
1.0
|
|
N
|
B:ASN215
|
4.3
|
20.2
|
1.0
|
|
N
|
B:LYS218
|
4.3
|
26.0
|
1.0
|
|
CB
|
B:ASP182
|
4.3
|
21.7
|
1.0
|
|
CB
|
B:ASN215
|
4.3
|
20.2
|
1.0
|
|
O3B
|
B:TPP900
|
4.4
|
26.4
|
1.0
|
|
O
|
B:HIS213
|
4.4
|
19.5
|
1.0
|
|
C
|
B:ASN215
|
4.4
|
20.2
|
1.0
|
|
CA
|
B:ASN215
|
4.6
|
20.2
|
1.0
|
|
C
|
B:GLY216
|
4.6
|
21.5
|
1.0
|
|
O2A
|
B:TPP900
|
4.7
|
26.4
|
1.0
|
|
CA
|
B:ASP182
|
4.7
|
21.7
|
1.0
|
|
O7
|
B:TPP900
|
4.8
|
26.4
|
1.0
|
|
CA
|
B:LYS218
|
4.8
|
26.0
|
1.0
|
|
CD
|
B:LYS300
|
4.8
|
21.9
|
1.0
|
|
C
|
B:ASP182
|
4.9
|
21.7
|
1.0
|
|
CE
|
B:LYS300
|
4.9
|
21.9
|
1.0
|
|
CA
|
B:GLY216
|
5.0
|
21.5
|
1.0
|
|
CB
|
B:TYR217
|
5.0
|
23.0
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 3 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg901
b:23.4
occ:1.00
|
O2B
|
C:TPP900
|
1.9
|
26.3
|
1.0
|
|
OD1
|
C:ASN215
|
2.0
|
20.2
|
1.0
|
|
OD1
|
C:ASP182
|
2.0
|
21.6
|
1.0
|
|
O
|
C:TYR217
|
2.2
|
22.9
|
1.0
|
|
O2A
|
C:TPP900
|
2.5
|
26.3
|
1.0
|
|
CG
|
C:ASP182
|
2.9
|
21.6
|
1.0
|
|
CG
|
C:ASN215
|
3.1
|
20.2
|
1.0
|
|
PB
|
C:TPP900
|
3.2
|
26.3
|
1.0
|
|
OD2
|
C:ASP182
|
3.2
|
21.6
|
1.0
|
|
C
|
C:TYR217
|
3.3
|
22.9
|
1.0
|
|
ND2
|
C:ASN215
|
3.6
|
20.2
|
1.0
|
|
N
|
C:TYR217
|
3.6
|
22.9
|
1.0
|
|
O3A
|
C:TPP900
|
3.7
|
26.3
|
1.0
|
|
PA
|
C:TPP900
|
3.7
|
26.3
|
1.0
|
|
O1B
|
C:TPP900
|
4.0
|
26.3
|
1.0
|
|
CA
|
C:TYR217
|
4.1
|
22.9
|
1.0
|
|
NZ
|
C:LYS300
|
4.1
|
21.9
|
1.0
|
|
N
|
C:GLY183
|
4.2
|
25.0
|
1.0
|
|
N
|
C:GLY216
|
4.2
|
21.5
|
1.0
|
|
N
|
C:ASP182
|
4.3
|
21.6
|
1.0
|
|
CG2
|
C:THR223
|
4.3
|
23.1
|
1.0
|
|
N
|
C:ASN215
|
4.3
|
20.2
|
1.0
|
|
N
|
C:LYS218
|
4.3
|
25.9
|
1.0
|
|
CB
|
C:ASP182
|
4.3
|
21.6
|
1.0
|
|
CB
|
C:ASN215
|
4.3
|
20.2
|
1.0
|
|
O3B
|
C:TPP900
|
4.4
|
26.3
|
1.0
|
|
O
|
C:HIS213
|
4.4
|
19.3
|
1.0
|
|
C
|
C:ASN215
|
4.4
|
20.2
|
1.0
|
|
CA
|
C:ASN215
|
4.6
|
20.2
|
1.0
|
|
C
|
C:GLY216
|
4.6
|
21.5
|
1.0
|
|
O1A
|
C:TPP900
|
4.7
|
26.3
|
1.0
|
|
CA
|
C:ASP182
|
4.7
|
21.6
|
1.0
|
|
O7
|
C:TPP900
|
4.8
|
26.3
|
1.0
|
|
CA
|
C:LYS218
|
4.8
|
25.9
|
1.0
|
|
CD
|
C:LYS300
|
4.8
|
21.9
|
1.0
|
|
C
|
C:ASP182
|
4.9
|
21.6
|
1.0
|
|
CE
|
C:LYS300
|
4.9
|
21.9
|
1.0
|
|
CA
|
C:GLY216
|
5.0
|
21.5
|
1.0
|
|
CB
|
C:TYR217
|
5.0
|
22.9
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 4 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg901
b:23.4
occ:1.00
|
O1B
|
D:TPP900
|
1.9
|
26.5
|
1.0
|
|
OD1
|
D:ASN215
|
2.0
|
20.2
|
1.0
|
|
OD1
|
D:ASP182
|
2.0
|
21.7
|
1.0
|
|
O
|
D:TYR217
|
2.2
|
23.1
|
1.0
|
|
O1A
|
D:TPP900
|
2.5
|
26.5
|
1.0
|
|
CG
|
D:ASP182
|
2.9
|
21.7
|
1.0
|
|
CG
|
D:ASN215
|
3.1
|
20.2
|
1.0
|
|
PB
|
D:TPP900
|
3.2
|
26.5
|
1.0
|
|
OD2
|
D:ASP182
|
3.2
|
21.7
|
1.0
|
|
C
|
D:TYR217
|
3.3
|
23.1
|
1.0
|
|
ND2
|
D:ASN215
|
3.6
|
20.2
|
1.0
|
|
N
|
D:TYR217
|
3.6
|
23.1
|
1.0
|
|
O3A
|
D:TPP900
|
3.7
|
26.5
|
1.0
|
|
PA
|
D:TPP900
|
3.7
|
26.5
|
1.0
|
|
O2B
|
D:TPP900
|
4.0
|
26.5
|
1.0
|
|
CA
|
D:TYR217
|
4.1
|
23.1
|
1.0
|
|
NZ
|
D:LYS300
|
4.1
|
21.9
|
1.0
|
|
N
|
D:GLY183
|
4.2
|
25.1
|
1.0
|
|
N
|
D:GLY216
|
4.2
|
21.7
|
1.0
|
|
N
|
D:ASP182
|
4.3
|
21.7
|
1.0
|
|
CG2
|
D:THR223
|
4.3
|
23.2
|
1.0
|
|
N
|
D:ASN215
|
4.3
|
20.2
|
1.0
|
|
N
|
D:LYS218
|
4.3
|
26.1
|
1.0
|
|
CB
|
D:ASP182
|
4.3
|
21.7
|
1.0
|
|
CB
|
D:ASN215
|
4.3
|
20.2
|
1.0
|
|
O3B
|
D:TPP900
|
4.4
|
26.5
|
1.0
|
|
O
|
D:HIS213
|
4.4
|
19.5
|
1.0
|
|
C
|
D:ASN215
|
4.4
|
20.2
|
1.0
|
|
CA
|
D:ASN215
|
4.6
|
20.2
|
1.0
|
|
C
|
D:GLY216
|
4.6
|
21.7
|
1.0
|
|
O2A
|
D:TPP900
|
4.7
|
26.5
|
1.0
|
|
CA
|
D:ASP182
|
4.7
|
21.7
|
1.0
|
|
O7
|
D:TPP900
|
4.8
|
26.5
|
1.0
|
|
CA
|
D:LYS218
|
4.8
|
26.1
|
1.0
|
|
CD
|
D:LYS300
|
4.8
|
21.9
|
1.0
|
|
C
|
D:ASP182
|
4.9
|
21.7
|
1.0
|
|
CE
|
D:LYS300
|
4.9
|
21.9
|
1.0
|
|
CA
|
D:GLY216
|
5.0
|
21.7
|
1.0
|
|
CB
|
D:TYR217
|
5.0
|
23.1
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 5 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg901
b:23.3
occ:1.00
|
O2B
|
E:TPP900
|
1.9
|
26.4
|
1.0
|
|
OD1
|
E:ASN215
|
2.0
|
20.1
|
1.0
|
|
OD1
|
E:ASP182
|
2.0
|
21.6
|
1.0
|
|
O
|
E:TYR217
|
2.2
|
22.9
|
1.0
|
|
O2A
|
E:TPP900
|
2.5
|
26.4
|
1.0
|
|
CG
|
E:ASP182
|
2.9
|
21.6
|
1.0
|
|
CG
|
E:ASN215
|
3.1
|
20.1
|
1.0
|
|
PB
|
E:TPP900
|
3.2
|
26.4
|
1.0
|
|
OD2
|
E:ASP182
|
3.2
|
21.6
|
1.0
|
|
C
|
E:TYR217
|
3.3
|
22.9
|
1.0
|
|
ND2
|
E:ASN215
|
3.6
|
20.1
|
1.0
|
|
N
|
E:TYR217
|
3.6
|
22.9
|
1.0
|
|
O3A
|
E:TPP900
|
3.7
|
26.4
|
1.0
|
|
PA
|
E:TPP900
|
3.7
|
26.4
|
1.0
|
|
O1B
|
E:TPP900
|
4.0
|
26.4
|
1.0
|
|
CA
|
E:TYR217
|
4.1
|
22.9
|
1.0
|
|
NZ
|
E:LYS300
|
4.1
|
21.8
|
1.0
|
|
N
|
E:GLY183
|
4.2
|
24.9
|
1.0
|
|
N
|
E:GLY216
|
4.2
|
21.6
|
1.0
|
|
N
|
E:ASP182
|
4.3
|
21.6
|
1.0
|
|
CG2
|
E:THR223
|
4.3
|
23.1
|
1.0
|
|
N
|
E:ASN215
|
4.3
|
20.1
|
1.0
|
|
N
|
E:LYS218
|
4.3
|
25.9
|
1.0
|
|
CB
|
E:ASP182
|
4.3
|
21.6
|
1.0
|
|
CB
|
E:ASN215
|
4.3
|
20.1
|
1.0
|
|
O3B
|
E:TPP900
|
4.4
|
26.4
|
1.0
|
|
O
|
E:HIS213
|
4.4
|
19.3
|
1.0
|
|
C
|
E:ASN215
|
4.4
|
20.1
|
1.0
|
|
CA
|
E:ASN215
|
4.6
|
20.1
|
1.0
|
|
C
|
E:GLY216
|
4.6
|
21.6
|
1.0
|
|
O1A
|
E:TPP900
|
4.7
|
26.4
|
1.0
|
|
CA
|
E:ASP182
|
4.7
|
21.6
|
1.0
|
|
O7
|
E:TPP900
|
4.8
|
26.4
|
1.0
|
|
CA
|
E:LYS218
|
4.8
|
25.9
|
1.0
|
|
CD
|
E:LYS300
|
4.8
|
21.8
|
1.0
|
|
C
|
E:ASP182
|
4.9
|
21.6
|
1.0
|
|
CE
|
E:LYS300
|
4.9
|
21.8
|
1.0
|
|
CA
|
E:GLY216
|
5.0
|
21.6
|
1.0
|
|
CB
|
E:TYR217
|
5.0
|
22.9
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 6 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg901
b:23.1
occ:1.00
|
O1B
|
F:TPP900
|
1.9
|
26.5
|
1.0
|
|
OD1
|
F:ASN215
|
2.0
|
20.1
|
1.0
|
|
OD1
|
F:ASP182
|
2.0
|
21.5
|
1.0
|
|
O
|
F:TYR217
|
2.2
|
22.9
|
1.0
|
|
O1A
|
F:TPP900
|
2.5
|
26.5
|
1.0
|
|
CG
|
F:ASP182
|
2.9
|
21.5
|
1.0
|
|
CG
|
F:ASN215
|
3.1
|
20.1
|
1.0
|
|
PB
|
F:TPP900
|
3.2
|
26.5
|
1.0
|
|
OD2
|
F:ASP182
|
3.2
|
21.5
|
1.0
|
|
C
|
F:TYR217
|
3.3
|
22.9
|
1.0
|
|
ND2
|
F:ASN215
|
3.6
|
20.1
|
1.0
|
|
N
|
F:TYR217
|
3.6
|
22.9
|
1.0
|
|
O3A
|
F:TPP900
|
3.7
|
26.5
|
1.0
|
|
PA
|
F:TPP900
|
3.7
|
26.5
|
1.0
|
|
O2B
|
F:TPP900
|
4.0
|
26.5
|
1.0
|
|
CA
|
F:TYR217
|
4.1
|
22.9
|
1.0
|
|
NZ
|
F:LYS300
|
4.1
|
21.9
|
1.0
|
|
N
|
F:GLY183
|
4.2
|
24.9
|
1.0
|
|
N
|
F:GLY216
|
4.2
|
21.5
|
1.0
|
|
N
|
F:ASP182
|
4.3
|
21.5
|
1.0
|
|
CG2
|
F:THR223
|
4.3
|
23.1
|
1.0
|
|
N
|
F:ASN215
|
4.3
|
20.1
|
1.0
|
|
N
|
F:LYS218
|
4.3
|
25.9
|
1.0
|
|
CB
|
F:ASP182
|
4.3
|
21.5
|
1.0
|
|
CB
|
F:ASN215
|
4.4
|
20.1
|
1.0
|
|
O3B
|
F:TPP900
|
4.4
|
26.5
|
1.0
|
|
O
|
F:HIS213
|
4.4
|
19.4
|
1.0
|
|
C
|
F:ASN215
|
4.4
|
20.1
|
1.0
|
|
CA
|
F:ASN215
|
4.6
|
20.1
|
1.0
|
|
C
|
F:GLY216
|
4.6
|
21.5
|
1.0
|
|
O2A
|
F:TPP900
|
4.7
|
26.5
|
1.0
|
|
CA
|
F:ASP182
|
4.7
|
21.5
|
1.0
|
|
O7
|
F:TPP900
|
4.8
|
26.5
|
1.0
|
|
CA
|
F:LYS218
|
4.8
|
25.9
|
1.0
|
|
CD
|
F:LYS300
|
4.8
|
21.9
|
1.0
|
|
C
|
F:ASP182
|
4.9
|
21.5
|
1.0
|
|
CE
|
F:LYS300
|
4.9
|
21.9
|
1.0
|
|
CA
|
F:GLY216
|
5.0
|
21.5
|
1.0
|
|
CB
|
F:TYR217
|
5.0
|
22.9
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 7 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg901
b:23.1
occ:1.00
|
O2B
|
G:TPP900
|
1.9
|
26.2
|
1.0
|
|
OD1
|
G:ASN215
|
2.0
|
20.0
|
1.0
|
|
OD1
|
G:ASP182
|
2.0
|
21.4
|
1.0
|
|
O
|
G:TYR217
|
2.2
|
22.8
|
1.0
|
|
O2A
|
G:TPP900
|
2.5
|
26.2
|
1.0
|
|
CG
|
G:ASP182
|
2.9
|
21.4
|
1.0
|
|
CG
|
G:ASN215
|
3.1
|
20.0
|
1.0
|
|
PB
|
G:TPP900
|
3.2
|
26.2
|
1.0
|
|
OD2
|
G:ASP182
|
3.2
|
21.4
|
1.0
|
|
C
|
G:TYR217
|
3.3
|
22.8
|
1.0
|
|
ND2
|
G:ASN215
|
3.6
|
20.0
|
1.0
|
|
N
|
G:TYR217
|
3.6
|
22.8
|
1.0
|
|
O3A
|
G:TPP900
|
3.7
|
26.2
|
1.0
|
|
PA
|
G:TPP900
|
3.7
|
26.2
|
1.0
|
|
O1B
|
G:TPP900
|
4.0
|
26.2
|
1.0
|
|
CA
|
G:TYR217
|
4.1
|
22.8
|
1.0
|
|
NZ
|
G:LYS300
|
4.1
|
21.8
|
1.0
|
|
N
|
G:GLY183
|
4.2
|
24.8
|
1.0
|
|
N
|
G:GLY216
|
4.2
|
21.5
|
1.0
|
|
N
|
G:ASP182
|
4.3
|
21.4
|
1.0
|
|
CG2
|
G:THR223
|
4.3
|
22.9
|
1.0
|
|
N
|
G:ASN215
|
4.3
|
20.0
|
1.0
|
|
N
|
G:LYS218
|
4.3
|
25.8
|
1.0
|
|
CB
|
G:ASP182
|
4.3
|
21.4
|
1.0
|
|
CB
|
G:ASN215
|
4.3
|
20.0
|
1.0
|
|
O3B
|
G:TPP900
|
4.4
|
26.2
|
1.0
|
|
O
|
G:HIS213
|
4.4
|
19.3
|
1.0
|
|
C
|
G:ASN215
|
4.4
|
20.0
|
1.0
|
|
CA
|
G:ASN215
|
4.6
|
20.0
|
1.0
|
|
C
|
G:GLY216
|
4.6
|
21.5
|
1.0
|
|
O1A
|
G:TPP900
|
4.7
|
26.2
|
1.0
|
|
CA
|
G:ASP182
|
4.7
|
21.4
|
1.0
|
|
O7
|
G:TPP900
|
4.8
|
26.2
|
1.0
|
|
CA
|
G:LYS218
|
4.8
|
25.8
|
1.0
|
|
CD
|
G:LYS300
|
4.8
|
21.8
|
1.0
|
|
C
|
G:ASP182
|
4.9
|
21.4
|
1.0
|
|
CE
|
G:LYS300
|
4.9
|
21.8
|
1.0
|
|
CA
|
G:GLY216
|
5.0
|
21.5
|
1.0
|
|
CB
|
G:TYR217
|
5.0
|
22.8
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 8io6
Go back to
Magnesium Binding Sites List in 8io6
Magnesium binding site 8 out
of 8 in the Cryo-Em Structure of Phosphoketolase From Bifidobacterium Longum in Octameric 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 Phosphoketolase From Bifidobacterium Longum in Octameric Assembly within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg901
b:23.0
occ:1.00
|
O1B
|
H:TPP900
|
1.9
|
26.6
|
1.0
|
|
OD1
|
H:ASN215
|
2.0
|
20.1
|
1.0
|
|
OD1
|
H:ASP182
|
2.0
|
21.6
|
1.0
|
|
O
|
H:TYR217
|
2.2
|
22.9
|
1.0
|
|
O1A
|
H:TPP900
|
2.5
|
26.6
|
1.0
|
|
CG
|
H:ASP182
|
2.9
|
21.6
|
1.0
|
|
CG
|
H:ASN215
|
3.1
|
20.1
|
1.0
|
|
PB
|
H:TPP900
|
3.2
|
26.6
|
1.0
|
|
OD2
|
H:ASP182
|
3.2
|
21.6
|
1.0
|
|
C
|
H:TYR217
|
3.3
|
22.9
|
1.0
|
|
ND2
|
H:ASN215
|
3.6
|
20.1
|
1.0
|
|
N
|
H:TYR217
|
3.6
|
22.9
|
1.0
|
|
O3A
|
H:TPP900
|
3.7
|
26.6
|
1.0
|
|
PA
|
H:TPP900
|
3.7
|
26.6
|
1.0
|
|
O2B
|
H:TPP900
|
4.0
|
26.6
|
1.0
|
|
CA
|
H:TYR217
|
4.1
|
22.9
|
1.0
|
|
NZ
|
H:LYS300
|
4.1
|
21.9
|
1.0
|
|
N
|
H:GLY183
|
4.2
|
24.9
|
1.0
|
|
N
|
H:GLY216
|
4.2
|
21.5
|
1.0
|
|
N
|
H:ASP182
|
4.3
|
21.6
|
1.0
|
|
CG2
|
H:THR223
|
4.3
|
23.0
|
1.0
|
|
N
|
H:ASN215
|
4.3
|
20.1
|
1.0
|
|
N
|
H:LYS218
|
4.3
|
25.9
|
1.0
|
|
CB
|
H:ASP182
|
4.3
|
21.6
|
1.0
|
|
CB
|
H:ASN215
|
4.3
|
20.1
|
1.0
|
|
O3B
|
H:TPP900
|
4.4
|
26.6
|
1.0
|
|
O
|
H:HIS213
|
4.4
|
19.4
|
1.0
|
|
C
|
H:ASN215
|
4.4
|
20.1
|
1.0
|
|
CA
|
H:ASN215
|
4.6
|
20.1
|
1.0
|
|
C
|
H:GLY216
|
4.6
|
21.5
|
1.0
|
|
O2A
|
H:TPP900
|
4.7
|
26.6
|
1.0
|
|
CA
|
H:ASP182
|
4.7
|
21.6
|
1.0
|
|
O7
|
H:TPP900
|
4.8
|
26.6
|
1.0
|
|
CA
|
H:LYS218
|
4.8
|
25.9
|
1.0
|
|
CD
|
H:LYS300
|
4.8
|
21.9
|
1.0
|
|
C
|
H:ASP182
|
4.9
|
21.6
|
1.0
|
|
CE
|
H:LYS300
|
4.9
|
21.9
|
1.0
|
|
CA
|
H:GLY216
|
5.0
|
21.5
|
1.0
|
|
CB
|
H:TYR217
|
5.0
|
22.9
|
1.0
|
|
Reference:
C.-W.Chang,
M.-D.Tsai.
An Atp-Sensitive Phosphoketolase Regulates Carbon Fixation in Cyanobacteria. Nat Metab 2023.
DOI: 10.1038/S42255-023-00831-W
Page generated: Fri Oct 4 09:29:45 2024
|
