Magnesium in PDB 8io8: Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly
(pdb code 8io8). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric Assembly, PDB code: 8io8:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 8io8
Go back to
Magnesium Binding Sites List in 8io8
Magnesium binding site 1 out
of 2 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric 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 Amppnpin Dimeric Assembly within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg803
b:76.9
occ:1.00
|
OD1
|
A:ASP178
|
2.1
|
73.3
|
1.0
|
O1A
|
A:TPP802
|
2.1
|
82.0
|
1.0
|
O
|
A:TYR213
|
2.1
|
78.9
|
1.0
|
O2B
|
A:TPP802
|
2.1
|
82.0
|
1.0
|
OD1
|
A:ASN211
|
2.1
|
72.3
|
1.0
|
CG
|
A:ASN211
|
3.0
|
72.3
|
1.0
|
CG
|
A:ASP178
|
3.0
|
73.3
|
1.0
|
PB
|
A:TPP802
|
3.2
|
82.0
|
1.0
|
ND2
|
A:ASN211
|
3.2
|
72.3
|
1.0
|
C
|
A:TYR213
|
3.3
|
78.9
|
1.0
|
PA
|
A:TPP802
|
3.3
|
82.0
|
1.0
|
OD2
|
A:ASP178
|
3.4
|
73.3
|
1.0
|
O3A
|
A:TPP802
|
3.4
|
82.0
|
1.0
|
O3B
|
A:TPP802
|
3.6
|
82.0
|
1.0
|
N
|
A:TYR213
|
4.0
|
78.9
|
1.0
|
N
|
A:ASP178
|
4.0
|
73.3
|
1.0
|
N
|
A:GLY179
|
4.1
|
73.4
|
1.0
|
CA
|
A:LYS214
|
4.1
|
80.8
|
1.0
|
N
|
A:LYS214
|
4.1
|
80.8
|
1.0
|
O7
|
A:TPP802
|
4.2
|
82.0
|
1.0
|
NZ
|
A:LYS293
|
4.3
|
74.8
|
1.0
|
CA
|
A:TYR213
|
4.3
|
78.9
|
1.0
|
O
|
A:HIS209
|
4.3
|
66.5
|
1.0
|
CB
|
A:ASP178
|
4.4
|
73.3
|
1.0
|
CG2
|
A:THR219
|
4.4
|
77.6
|
1.0
|
CB
|
A:ASN211
|
4.4
|
72.3
|
1.0
|
O2A
|
A:TPP802
|
4.4
|
82.0
|
1.0
|
O1B
|
A:TPP802
|
4.5
|
82.0
|
1.0
|
N
|
A:ASN211
|
4.5
|
72.3
|
1.0
|
CA
|
A:ASP178
|
4.6
|
73.3
|
1.0
|
N
|
A:GLY212
|
4.7
|
74.8
|
1.0
|
C
|
A:ASP178
|
4.8
|
73.3
|
1.0
|
CE
|
A:LYS293
|
4.8
|
74.8
|
1.0
|
CA
|
A:ASN211
|
4.8
|
72.3
|
1.0
|
CD
|
A:LYS293
|
4.8
|
74.8
|
1.0
|
CB
|
A:LYS214
|
4.9
|
80.8
|
1.0
|
C
|
A:GLY177
|
4.9
|
68.9
|
1.0
|
C
|
A:ASN211
|
4.9
|
72.3
|
1.0
|
CA
|
A:GLY179
|
5.0
|
73.4
|
1.0
|
CA
|
A:GLY177
|
5.0
|
68.9
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 8io8
Go back to
Magnesium Binding Sites List in 8io8
Magnesium binding site 2 out
of 2 in the Cryo-Em Structure of Cyanobacteria Phosphoketolase Complexed with Amppnpin Dimeric 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 Amppnpin Dimeric Assembly within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg803
b:76.6
occ:1.00
|
OD1
|
B:ASP178
|
2.0
|
74.0
|
1.0
|
O
|
B:TYR213
|
2.0
|
78.8
|
1.0
|
O3B
|
B:TPP802
|
2.0
|
83.2
|
1.0
|
OD1
|
B:ASN211
|
2.2
|
72.3
|
1.0
|
O2A
|
B:TPP802
|
2.4
|
83.2
|
1.0
|
PB
|
B:TPP802
|
2.8
|
83.2
|
1.0
|
CG
|
B:ASP178
|
3.0
|
74.0
|
1.0
|
O2B
|
B:TPP802
|
3.1
|
83.2
|
1.0
|
CG
|
B:ASN211
|
3.1
|
72.3
|
1.0
|
C
|
B:TYR213
|
3.2
|
78.8
|
1.0
|
O3A
|
B:TPP802
|
3.2
|
83.2
|
1.0
|
ND2
|
B:ASN211
|
3.3
|
72.3
|
1.0
|
OD2
|
B:ASP178
|
3.3
|
74.0
|
1.0
|
PA
|
B:TPP802
|
3.4
|
83.2
|
1.0
|
CA
|
B:LYS214
|
4.0
|
81.7
|
1.0
|
N
|
B:LYS214
|
4.0
|
81.7
|
1.0
|
N
|
B:TYR213
|
4.1
|
78.8
|
1.0
|
N
|
B:ASP178
|
4.1
|
74.0
|
1.0
|
N
|
B:GLY179
|
4.1
|
74.2
|
1.0
|
NZ
|
B:LYS293
|
4.2
|
73.9
|
1.0
|
O1B
|
B:TPP802
|
4.3
|
83.2
|
1.0
|
CA
|
B:TYR213
|
4.3
|
78.8
|
1.0
|
CB
|
B:ASP178
|
4.4
|
74.0
|
1.0
|
O7
|
B:TPP802
|
4.4
|
83.2
|
1.0
|
CG2
|
B:THR219
|
4.4
|
77.8
|
1.0
|
O1A
|
B:TPP802
|
4.5
|
83.2
|
1.0
|
O
|
B:HIS209
|
4.5
|
66.9
|
1.0
|
CB
|
B:ASN211
|
4.5
|
72.3
|
1.0
|
CE
|
B:LYS293
|
4.7
|
73.9
|
1.0
|
CA
|
B:ASP178
|
4.7
|
74.0
|
1.0
|
N
|
B:ASN211
|
4.7
|
72.3
|
1.0
|
N
|
B:GLY212
|
4.8
|
75.4
|
1.0
|
CB
|
B:LYS214
|
4.8
|
81.7
|
1.0
|
CD
|
B:LYS293
|
4.8
|
73.9
|
1.0
|
C
|
B:ASP178
|
4.9
|
74.0
|
1.0
|
CA
|
B:ASN211
|
5.0
|
72.3
|
1.0
|
O
|
B:LYS214
|
5.0
|
81.7
|
1.0
|
C
|
B:GLY177
|
5.0
|
69.6
|
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 Oct 4 09:29:44 2024
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