Magnesium in PDB 8i3i: Acyl-Acp Synthetase Structure Bound to Amp-Pnp
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Acyl-Acp Synthetase Structure Bound to Amp-Pnp
(pdb code 8i3i). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Acyl-Acp Synthetase Structure Bound to Amp-Pnp, PDB code: 8i3i:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 8i3i
Go back to
Magnesium Binding Sites List in 8i3i
Magnesium binding site 1 out
of 4 in the Acyl-Acp Synthetase Structure Bound to Amp-Pnp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Acyl-Acp Synthetase Structure Bound to Amp-Pnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1001
b:49.7
occ:1.00
|
O2G
|
A:ANP1002
|
2.2
|
51.4
|
1.0
|
O2B
|
A:ANP1002
|
2.6
|
51.3
|
1.0
|
PG
|
A:ANP1002
|
3.5
|
49.8
|
1.0
|
O2A
|
A:ANP1002
|
3.8
|
53.7
|
1.0
|
PB
|
A:ANP1002
|
3.8
|
45.1
|
1.0
|
N3B
|
A:ANP1002
|
3.8
|
52.8
|
1.0
|
CE
|
A:MET320
|
4.1
|
52.3
|
1.0
|
O1G
|
A:ANP1002
|
4.1
|
53.1
|
1.0
|
O3'
|
A:ANP1002
|
4.2
|
57.4
|
1.0
|
O5'
|
A:ANP1002
|
4.3
|
57.3
|
1.0
|
OE2
|
A:GLU322
|
4.3
|
56.7
|
1.0
|
NH1
|
A:ARG426
|
4.5
|
55.4
|
1.0
|
PA
|
A:ANP1002
|
4.5
|
54.4
|
1.0
|
O3A
|
A:ANP1002
|
4.6
|
57.6
|
1.0
|
O3G
|
A:ANP1002
|
4.7
|
57.8
|
1.0
|
O
|
A:MET320
|
4.8
|
63.7
|
1.0
|
NZ
|
A:LYS183
|
4.8
|
51.2
|
1.0
|
O1B
|
A:ANP1002
|
4.9
|
54.1
|
1.0
|
CD
|
A:GLU322
|
4.9
|
53.6
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 8i3i
Go back to
Magnesium Binding Sites List in 8i3i
Magnesium binding site 2 out
of 4 in the Acyl-Acp Synthetase Structure Bound to Amp-Pnp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Acyl-Acp Synthetase Structure Bound to Amp-Pnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1001
b:49.7
occ:1.00
|
O2G
|
D:ANP1002
|
2.2
|
51.4
|
1.0
|
O2B
|
D:ANP1002
|
2.6
|
51.3
|
1.0
|
PG
|
D:ANP1002
|
3.5
|
49.8
|
1.0
|
O2A
|
D:ANP1002
|
3.8
|
53.7
|
1.0
|
PB
|
D:ANP1002
|
3.8
|
45.1
|
1.0
|
N3B
|
D:ANP1002
|
3.8
|
52.8
|
1.0
|
CE
|
D:MET320
|
4.1
|
52.3
|
1.0
|
O1G
|
D:ANP1002
|
4.1
|
53.1
|
1.0
|
O3'
|
D:ANP1002
|
4.2
|
57.4
|
1.0
|
O5'
|
D:ANP1002
|
4.3
|
57.3
|
1.0
|
OE2
|
D:GLU322
|
4.3
|
56.7
|
1.0
|
NH1
|
D:ARG426
|
4.5
|
55.4
|
1.0
|
PA
|
D:ANP1002
|
4.5
|
54.4
|
1.0
|
O3A
|
D:ANP1002
|
4.6
|
57.6
|
1.0
|
O3G
|
D:ANP1002
|
4.7
|
57.8
|
1.0
|
O
|
D:MET320
|
4.8
|
63.7
|
1.0
|
NZ
|
D:LYS183
|
4.8
|
51.2
|
1.0
|
O1B
|
D:ANP1002
|
4.9
|
54.1
|
1.0
|
CD
|
D:GLU322
|
4.9
|
53.6
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 8i3i
Go back to
Magnesium Binding Sites List in 8i3i
Magnesium binding site 3 out
of 4 in the Acyl-Acp Synthetase Structure Bound to Amp-Pnp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Acyl-Acp Synthetase Structure Bound to Amp-Pnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1001
b:49.7
occ:1.00
|
O2G
|
B:ANP1002
|
2.2
|
51.4
|
1.0
|
O2B
|
B:ANP1002
|
2.6
|
51.3
|
1.0
|
PG
|
B:ANP1002
|
3.5
|
49.8
|
1.0
|
O2A
|
B:ANP1002
|
3.8
|
53.7
|
1.0
|
PB
|
B:ANP1002
|
3.8
|
45.1
|
1.0
|
N3B
|
B:ANP1002
|
3.8
|
52.8
|
1.0
|
CE
|
B:MET320
|
4.1
|
52.3
|
1.0
|
O1G
|
B:ANP1002
|
4.1
|
53.1
|
1.0
|
O3'
|
B:ANP1002
|
4.2
|
57.4
|
1.0
|
O5'
|
B:ANP1002
|
4.3
|
57.3
|
1.0
|
OE2
|
B:GLU322
|
4.3
|
56.7
|
1.0
|
NH1
|
B:ARG426
|
4.5
|
55.4
|
1.0
|
PA
|
B:ANP1002
|
4.5
|
54.4
|
1.0
|
O3A
|
B:ANP1002
|
4.6
|
57.6
|
1.0
|
O3G
|
B:ANP1002
|
4.7
|
57.8
|
1.0
|
O
|
B:MET320
|
4.8
|
63.7
|
1.0
|
NZ
|
B:LYS183
|
4.8
|
51.2
|
1.0
|
O1B
|
B:ANP1002
|
4.9
|
54.1
|
1.0
|
CD
|
B:GLU322
|
4.9
|
53.6
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 8i3i
Go back to
Magnesium Binding Sites List in 8i3i
Magnesium binding site 4 out
of 4 in the Acyl-Acp Synthetase Structure Bound to Amp-Pnp
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Acyl-Acp Synthetase Structure Bound to Amp-Pnp within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1001
b:49.7
occ:1.00
|
O2G
|
C:ANP1002
|
2.2
|
51.4
|
1.0
|
O2B
|
C:ANP1002
|
2.6
|
51.3
|
1.0
|
PG
|
C:ANP1002
|
3.5
|
49.8
|
1.0
|
O2A
|
C:ANP1002
|
3.8
|
53.7
|
1.0
|
PB
|
C:ANP1002
|
3.8
|
45.1
|
1.0
|
N3B
|
C:ANP1002
|
3.8
|
52.8
|
1.0
|
CE
|
C:MET320
|
4.1
|
52.3
|
1.0
|
O1G
|
C:ANP1002
|
4.1
|
53.1
|
1.0
|
O3'
|
C:ANP1002
|
4.2
|
57.4
|
1.0
|
O5'
|
C:ANP1002
|
4.3
|
57.3
|
1.0
|
OE2
|
C:GLU322
|
4.3
|
56.7
|
1.0
|
NH1
|
C:ARG426
|
4.5
|
55.4
|
1.0
|
PA
|
C:ANP1002
|
4.5
|
54.4
|
1.0
|
O3A
|
C:ANP1002
|
4.6
|
57.6
|
1.0
|
O3G
|
C:ANP1002
|
4.7
|
57.8
|
1.0
|
O
|
C:MET320
|
4.8
|
63.7
|
1.0
|
NZ
|
C:LYS183
|
4.8
|
51.2
|
1.0
|
O1B
|
C:ANP1002
|
4.9
|
54.1
|
1.0
|
CD
|
C:GLU322
|
4.9
|
53.6
|
1.0
|
|
Reference:
H.Huang,
C.Wang,
S.Chang,
T.Cui,
Y.Xu,
H.Zhang,
C.Zhou,
X.Zhang,
Y.Feng.
Acyl-Acp Synthetase Structure Bound to Amp-Pnp To Be Published.
Page generated: Fri Oct 4 09:06:26 2024
|