Magnesium in PDB 5mcp: Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
Enzymatic activity of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
All present enzymatic activity of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp:
1.1.1.205;
Protein crystallography data
The structure of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp, PDB code: 5mcp
was solved by
G.Winter,
D.Fernandez-Justel,
J.M.De Pereda,
J.L.Revuelta,
R.M.Buey,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
152.04 /
2.40
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
127.891,
152.090,
152.255,
90.00,
93.03,
90.00
|
|
R / Rfree (%)
|
24.9 /
27.1
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
(pdb code 5mcp). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp, PDB code: 5mcp:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 1 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg604
b:79.3
occ:1.00
|
O1G
|
B:ATP605
|
1.8
|
0.3
|
1.0
|
|
O3B
|
B:ATP606
|
2.1
|
0.5
|
1.0
|
|
OE1
|
B:GLN170
|
3.0
|
0.7
|
1.0
|
|
PG
|
B:ATP605
|
3.2
|
0.8
|
1.0
|
|
PB
|
B:ATP606
|
3.2
|
0.3
|
1.0
|
|
O3G
|
B:ATP606
|
3.4
|
0.1
|
1.0
|
|
PG
|
B:ATP606
|
3.4
|
0.5
|
1.0
|
|
O1B
|
B:ATP605
|
3.4
|
0.1
|
1.0
|
|
O3A
|
B:ATP606
|
3.5
|
0.9
|
1.0
|
|
O2B
|
B:ATP606
|
3.6
|
0.8
|
1.0
|
|
PA
|
B:ATP606
|
3.7
|
0.0
|
1.0
|
|
O2G
|
B:ATP605
|
3.7
|
0.1
|
1.0
|
|
HE22
|
B:GLN170
|
3.8
|
0.5
|
1.0
|
|
O1A
|
B:ATP606
|
3.8
|
0.8
|
1.0
|
|
O2G
|
B:ATP606
|
3.9
|
0.3
|
1.0
|
|
CD
|
B:GLN170
|
4.0
|
0.2
|
1.0
|
|
PB
|
B:ATP605
|
4.0
|
0.9
|
1.0
|
|
O3B
|
B:ATP605
|
4.2
|
0.5
|
1.0
|
|
NE2
|
B:GLN170
|
4.3
|
0.1
|
1.0
|
|
O3G
|
B:ATP605
|
4.3
|
0.1
|
1.0
|
|
O2A
|
B:ATP606
|
4.3
|
0.1
|
1.0
|
|
O1B
|
B:ATP606
|
4.5
|
0.3
|
1.0
|
|
O1G
|
B:ATP606
|
4.5
|
0.0
|
1.0
|
|
O2B
|
B:ATP605
|
4.7
|
0.3
|
1.0
|
|
HG
|
F:SER166
|
4.9
|
0.4
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 2 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg604
b:89.2
occ:1.00
|
O2B
|
C:ATP602
|
1.8
|
93.3
|
1.0
|
|
O2G
|
C:ATP602
|
2.4
|
60.7
|
1.0
|
|
O2G
|
C:ATP601
|
2.6
|
70.9
|
1.0
|
|
O2B
|
C:ATP601
|
2.6
|
70.2
|
1.0
|
|
HZ3
|
C:LYS210
|
2.9
|
66.9
|
1.0
|
|
PB
|
C:ATP602
|
3.1
|
76.1
|
1.0
|
|
HZ1
|
C:LYS210
|
3.2
|
66.9
|
1.0
|
|
HE22
|
H:GLN170
|
3.2
|
0.3
|
1.0
|
|
NZ
|
C:LYS210
|
3.4
|
55.7
|
1.0
|
|
HE3
|
C:LYS210
|
3.5
|
65.6
|
1.0
|
|
PB
|
C:ATP601
|
3.5
|
71.2
|
1.0
|
|
PG
|
C:ATP602
|
3.6
|
63.4
|
1.0
|
|
PG
|
C:ATP601
|
3.7
|
72.0
|
1.0
|
|
O
|
C:HOH808
|
3.7
|
47.8
|
1.0
|
|
PA
|
C:ATP602
|
3.8
|
55.1
|
1.0
|
|
O1A
|
C:ATP602
|
3.8
|
53.5
|
1.0
|
|
O3B
|
C:ATP602
|
3.9
|
70.7
|
1.0
|
|
O2A
|
C:ATP602
|
3.9
|
54.9
|
1.0
|
|
HZ
|
H:PHE171
|
3.9
|
0.8
|
1.0
|
|
NE2
|
H:GLN170
|
4.0
|
98.6
|
1.0
|
|
CE
|
C:LYS210
|
4.0
|
54.6
|
1.0
|
|
O1G
|
C:ATP601
|
4.0
|
71.6
|
1.0
|
|
O3B
|
C:ATP601
|
4.1
|
72.2
|
1.0
|
|
O3A
|
C:ATP602
|
4.1
|
65.5
|
1.0
|
|
O1B
|
C:ATP602
|
4.2
|
72.7
|
1.0
|
|
HZ2
|
C:LYS210
|
4.2
|
66.9
|
1.0
|
|
O
|
C:HOH708
|
4.2
|
42.4
|
1.0
|
|
O1B
|
C:ATP601
|
4.3
|
71.7
|
1.0
|
|
HA3
|
C:GLY209
|
4.4
|
69.9
|
1.0
|
|
HE21
|
H:GLN170
|
4.4
|
0.3
|
1.0
|
|
O3G
|
C:ATP602
|
4.4
|
60.0
|
1.0
|
|
HE2
|
C:LYS210
|
4.5
|
65.6
|
1.0
|
|
HG1
|
C:THR227
|
4.6
|
89.5
|
1.0
|
|
OE1
|
H:GLN170
|
4.7
|
99.4
|
1.0
|
|
CD
|
H:GLN170
|
4.8
|
99.1
|
1.0
|
|
O1A
|
C:ATP601
|
4.8
|
69.0
|
1.0
|
|
O1G
|
C:ATP602
|
4.8
|
61.7
|
1.0
|
|
CZ
|
H:PHE171
|
4.8
|
89.7
|
1.0
|
|
PA
|
C:ATP601
|
4.9
|
69.7
|
1.0
|
|
HE2
|
H:PHE171
|
4.9
|
0.5
|
1.0
|
|
O
|
C:HOH800
|
4.9
|
57.1
|
1.0
|
|
O3A
|
C:ATP601
|
4.9
|
71.0
|
1.0
|
|
OG1
|
C:THR227
|
4.9
|
74.5
|
1.0
|
|
HD3
|
C:LYS210
|
5.0
|
62.6
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 3 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg605
b:0.2
occ:1.00
|
O1B
|
H:ATP601
|
2.3
|
0.1
|
1.0
|
|
O3B
|
H:ATP602
|
2.6
|
97.0
|
0.9
|
|
O2G
|
H:ATP601
|
2.7
|
0.6
|
1.0
|
|
PB
|
H:ATP601
|
2.9
|
97.8
|
1.0
|
|
O3G
|
H:ATP601
|
3.0
|
0.1
|
1.0
|
|
PG
|
H:ATP601
|
3.2
|
0.7
|
1.0
|
|
O2G
|
H:ATP602
|
3.2
|
0.2
|
0.9
|
|
PG
|
H:ATP602
|
3.4
|
98.6
|
0.9
|
|
HE22
|
C:GLN170
|
3.4
|
0.4
|
1.0
|
|
O2B
|
H:ATP601
|
3.5
|
98.3
|
1.0
|
|
O3B
|
H:ATP601
|
3.5
|
0.5
|
1.0
|
|
PB
|
H:ATP602
|
3.7
|
99.3
|
0.9
|
|
O1G
|
H:ATP602
|
3.7
|
95.5
|
0.9
|
|
O3A
|
H:ATP602
|
3.9
|
98.5
|
0.9
|
|
O2B
|
H:ATP602
|
4.1
|
99.4
|
0.9
|
|
NE2
|
C:GLN170
|
4.2
|
0.6
|
1.0
|
|
OE1
|
C:GLN170
|
4.3
|
0.6
|
1.0
|
|
PA
|
H:ATP602
|
4.3
|
98.0
|
0.9
|
|
HG
|
H:SER166
|
4.4
|
0.2
|
1.0
|
|
O3A
|
H:ATP601
|
4.4
|
97.3
|
1.0
|
|
PA
|
H:ATP601
|
4.6
|
96.8
|
1.0
|
|
CD
|
C:GLN170
|
4.7
|
0.1
|
1.0
|
|
O1G
|
H:ATP601
|
4.7
|
0.4
|
1.0
|
|
O3G
|
H:ATP602
|
4.7
|
95.7
|
0.9
|
|
O1A
|
H:ATP602
|
4.7
|
98.2
|
0.9
|
|
HZ
|
C:PHE171
|
4.8
|
0.2
|
1.0
|
|
O2A
|
H:ATP602
|
4.8
|
97.3
|
0.9
|
|
HE21
|
C:GLN170
|
4.8
|
0.4
|
1.0
|
|
O1A
|
H:ATP601
|
4.8
|
97.7
|
1.0
|
|
HA3
|
H:GLY209
|
4.8
|
0.2
|
1.0
|
|
O2A
|
H:ATP601
|
4.9
|
96.2
|
1.0
|
|
OG
|
H:SER166
|
4.9
|
0.8
|
1.0
|
|
O1B
|
H:ATP602
|
5.0
|
99.9
|
0.9
|
|
Magnesium binding site 4 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 4 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg604
b:87.5
occ:1.00
|
O3G
|
G:ATP601
|
1.9
|
98.0
|
1.0
|
|
O1B
|
G:ATP601
|
1.9
|
97.2
|
1.0
|
|
O1G
|
G:ATP602
|
2.0
|
0.4
|
1.0
|
|
O1B
|
G:ATP602
|
2.4
|
0.7
|
1.0
|
|
PB
|
G:ATP601
|
2.8
|
89.3
|
1.0
|
|
PG
|
G:ATP601
|
3.3
|
91.6
|
1.0
|
|
HE22
|
D:GLN170
|
3.3
|
0.8
|
1.0
|
|
PG
|
G:ATP602
|
3.4
|
0.5
|
1.0
|
|
O2B
|
G:ATP601
|
3.5
|
84.1
|
1.0
|
|
O3B
|
G:ATP601
|
3.6
|
90.2
|
1.0
|
|
PB
|
G:ATP602
|
3.6
|
1.0
|
1.0
|
|
O3B
|
G:ATP602
|
4.1
|
1.0
|
1.0
|
|
O3A
|
G:ATP602
|
4.1
|
0.5
|
1.0
|
|
O2G
|
G:ATP602
|
4.1
|
0.9
|
1.0
|
|
NE2
|
D:GLN170
|
4.2
|
0.9
|
1.0
|
|
O3A
|
G:ATP601
|
4.2
|
85.1
|
1.0
|
|
O1G
|
G:ATP601
|
4.2
|
94.5
|
1.0
|
|
O1A
|
G:ATP602
|
4.2
|
0.3
|
1.0
|
|
O2G
|
G:ATP601
|
4.3
|
93.7
|
1.0
|
|
PA
|
G:ATP601
|
4.3
|
84.8
|
1.0
|
|
O1A
|
G:ATP601
|
4.5
|
83.0
|
1.0
|
|
PA
|
G:ATP602
|
4.5
|
0.6
|
1.0
|
|
O3G
|
G:ATP602
|
4.5
|
0.8
|
1.0
|
|
OE1
|
D:GLN170
|
4.6
|
0.8
|
1.0
|
|
HZ
|
D:PHE171
|
4.6
|
0.7
|
1.0
|
|
HA3
|
G:GLY209
|
4.7
|
0.4
|
1.0
|
|
HE21
|
D:GLN170
|
4.7
|
0.8
|
1.0
|
|
O2A
|
G:ATP601
|
4.8
|
86.3
|
1.0
|
|
CD
|
D:GLN170
|
4.8
|
0.0
|
1.0
|
|
HB
|
G:THR165
|
4.9
|
0.1
|
1.0
|
|
O2B
|
G:ATP602
|
5.0
|
0.9
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 5 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg604
b:86.7
occ:1.00
|
O1B
|
A:ATP602
|
1.9
|
62.1
|
1.0
|
|
O3G
|
A:ATP602
|
1.9
|
64.5
|
1.0
|
|
O3G
|
A:ATP601
|
2.2
|
64.0
|
1.0
|
|
O1B
|
A:ATP601
|
2.2
|
66.1
|
1.0
|
|
HE22
|
E:GLN170
|
2.9
|
0.9
|
1.0
|
|
PB
|
A:ATP602
|
3.1
|
60.6
|
1.0
|
|
HZ1
|
A:LYS210
|
3.1
|
94.1
|
1.0
|
|
HZ2
|
A:LYS210
|
3.2
|
94.1
|
1.0
|
|
PB
|
A:ATP601
|
3.2
|
65.1
|
1.0
|
|
PG
|
A:ATP602
|
3.3
|
67.4
|
1.0
|
|
PG
|
A:ATP601
|
3.6
|
64.9
|
1.0
|
|
NZ
|
A:LYS210
|
3.6
|
78.4
|
1.0
|
|
O3B
|
A:ATP602
|
3.6
|
61.7
|
1.0
|
|
NE2
|
E:GLN170
|
3.7
|
0.7
|
1.0
|
|
O1A
|
A:ATP602
|
3.7
|
55.2
|
1.0
|
|
O3B
|
A:ATP601
|
3.9
|
64.5
|
1.0
|
|
O
|
A:HOH724
|
3.9
|
49.5
|
1.0
|
|
HE3
|
A:LYS210
|
3.9
|
92.7
|
1.0
|
|
O2B
|
A:ATP601
|
4.0
|
63.4
|
1.0
|
|
O1G
|
A:ATP602
|
4.0
|
66.0
|
1.0
|
|
HE21
|
E:GLN170
|
4.1
|
0.9
|
1.0
|
|
HZ
|
E:PHE171
|
4.1
|
99.0
|
1.0
|
|
PA
|
A:ATP602
|
4.1
|
52.5
|
1.0
|
|
O2B
|
A:ATP602
|
4.2
|
59.3
|
1.0
|
|
O3A
|
A:ATP602
|
4.2
|
58.8
|
1.0
|
|
HZ3
|
A:LYS210
|
4.3
|
94.1
|
1.0
|
|
O2G
|
A:ATP601
|
4.3
|
64.7
|
1.0
|
|
CE
|
A:LYS210
|
4.4
|
77.2
|
1.0
|
|
OE1
|
E:GLN170
|
4.4
|
99.6
|
1.0
|
|
CD
|
E:GLN170
|
4.5
|
0.3
|
1.0
|
|
O2G
|
A:ATP602
|
4.5
|
68.9
|
1.0
|
|
HA3
|
A:GLY209
|
4.5
|
75.2
|
1.0
|
|
O3A
|
A:ATP601
|
4.5
|
61.4
|
1.0
|
|
O1G
|
A:ATP601
|
4.7
|
66.3
|
1.0
|
|
PA
|
A:ATP601
|
4.7
|
58.1
|
1.0
|
|
O2A
|
A:ATP602
|
4.8
|
53.7
|
1.0
|
|
HG23
|
A:THR227
|
4.8
|
84.2
|
1.0
|
|
HG21
|
A:THR227
|
4.8
|
84.2
|
1.0
|
|
O2A
|
A:ATP601
|
4.9
|
59.0
|
1.0
|
|
HE2
|
A:LYS210
|
4.9
|
92.7
|
1.0
|
|
CZ
|
E:PHE171
|
5.0
|
82.4
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 6 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg605
b:93.4
occ:1.00
|
O2G
|
E:ATP602
|
1.8
|
0.5
|
1.0
|
|
O1G
|
E:ATP601
|
2.0
|
95.5
|
1.0
|
|
O2B
|
E:ATP602
|
2.0
|
0.3
|
1.0
|
|
O2B
|
E:ATP601
|
2.1
|
94.4
|
1.0
|
|
PG
|
E:ATP602
|
3.2
|
0.5
|
1.0
|
|
PB
|
E:ATP602
|
3.2
|
0.6
|
1.0
|
|
PG
|
E:ATP601
|
3.2
|
92.0
|
1.0
|
|
PB
|
E:ATP601
|
3.3
|
91.1
|
1.0
|
|
O3B
|
E:ATP602
|
3.7
|
0.7
|
1.0
|
|
O3B
|
E:ATP601
|
3.7
|
91.7
|
1.0
|
|
O2G
|
E:ATP601
|
3.7
|
89.6
|
1.0
|
|
O
|
E:HOH725
|
3.8
|
51.2
|
1.0
|
|
O3A
|
E:ATP601
|
3.9
|
88.9
|
1.0
|
|
O3G
|
E:ATP602
|
4.2
|
0.2
|
1.0
|
|
O1G
|
E:ATP602
|
4.2
|
0.5
|
1.0
|
|
O2A
|
E:ATP602
|
4.2
|
0.5
|
1.0
|
|
O1B
|
E:ATP602
|
4.3
|
0.8
|
1.0
|
|
PA
|
E:ATP602
|
4.3
|
0.3
|
1.0
|
|
O3A
|
E:ATP602
|
4.4
|
0.9
|
1.0
|
|
O3G
|
E:ATP601
|
4.5
|
90.6
|
1.0
|
|
O1B
|
E:ATP601
|
4.7
|
90.6
|
1.0
|
|
O1A
|
E:ATP602
|
4.7
|
0.6
|
1.0
|
|
HG
|
E:SER166
|
4.7
|
0.1
|
1.0
|
|
O1A
|
E:ATP601
|
4.8
|
87.0
|
1.0
|
|
PA
|
E:ATP601
|
4.9
|
85.9
|
1.0
|
|
HA3
|
E:GLY209
|
4.9
|
0.7
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 7 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg602
b:95.8
occ:1.00
|
O2B
|
B:ATP602
|
1.9
|
62.8
|
1.0
|
|
O1G
|
B:ATP601
|
2.0
|
71.1
|
1.0
|
|
O2G
|
B:ATP602
|
2.1
|
68.0
|
1.0
|
|
O2B
|
B:ATP601
|
2.7
|
70.1
|
1.0
|
|
HE21
|
F:GLN170
|
2.9
|
0.9
|
1.0
|
|
HZ1
|
B:LYS210
|
3.0
|
80.5
|
1.0
|
|
PB
|
B:ATP602
|
3.0
|
64.0
|
1.0
|
|
PG
|
B:ATP602
|
3.3
|
67.5
|
1.0
|
|
PG
|
B:ATP601
|
3.5
|
71.4
|
1.0
|
|
O3B
|
B:ATP602
|
3.5
|
66.8
|
1.0
|
|
PB
|
B:ATP601
|
3.5
|
67.8
|
1.0
|
|
HE3
|
B:LYS210
|
3.6
|
78.7
|
1.0
|
|
HZ2
|
B:LYS210
|
3.6
|
80.5
|
1.0
|
|
NZ
|
B:LYS210
|
3.6
|
67.0
|
1.0
|
|
NE2
|
F:GLN170
|
3.7
|
90.7
|
1.0
|
|
O
|
B:HOH774
|
4.0
|
29.3
|
1.0
|
|
O1B
|
B:ATP602
|
4.1
|
66.4
|
1.0
|
|
O3B
|
B:ATP601
|
4.1
|
70.0
|
1.0
|
|
CE
|
B:LYS210
|
4.1
|
65.5
|
1.0
|
|
PA
|
B:ATP602
|
4.1
|
59.7
|
1.0
|
|
O1B
|
B:ATP601
|
4.1
|
66.3
|
1.0
|
|
O2A
|
B:ATP602
|
4.2
|
62.5
|
1.0
|
|
HE22
|
F:GLN170
|
4.2
|
0.9
|
1.0
|
|
O3A
|
B:ATP602
|
4.2
|
61.4
|
1.0
|
|
O1G
|
B:ATP602
|
4.2
|
67.7
|
1.0
|
|
O1A
|
B:ATP602
|
4.3
|
58.8
|
1.0
|
|
O2G
|
B:ATP601
|
4.3
|
72.0
|
1.0
|
|
HZ
|
F:PHE171
|
4.4
|
94.0
|
1.0
|
|
HZ3
|
B:LYS210
|
4.4
|
80.5
|
1.0
|
|
O3G
|
B:ATP601
|
4.4
|
72.2
|
1.0
|
|
O3G
|
B:ATP602
|
4.4
|
68.4
|
1.0
|
|
HE2
|
B:LYS210
|
4.4
|
78.7
|
1.0
|
|
OE1
|
F:GLN170
|
4.4
|
91.8
|
1.0
|
|
CD
|
F:GLN170
|
4.5
|
91.3
|
1.0
|
|
O
|
B:HOH727
|
4.5
|
52.0
|
1.0
|
|
HG21
|
B:THR227
|
4.7
|
85.7
|
1.0
|
|
HG23
|
B:THR227
|
4.8
|
85.7
|
1.0
|
|
HA3
|
B:GLY209
|
4.9
|
80.8
|
1.0
|
|
O3A
|
B:ATP601
|
5.0
|
66.2
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 5mcp
Go back to
Magnesium Binding Sites List in 5mcp
Magnesium binding site 8 out
of 8 in the Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Structure of Imp Dehydrogenase From Ashbya Gossypii Bound to Atp within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg604
b:64.2
occ:1.00
|
O3B
|
D:ATP602
|
2.3
|
68.2
|
1.0
|
|
O2B
|
D:ATP601
|
2.3
|
75.8
|
1.0
|
|
O1G
|
D:ATP602
|
2.7
|
62.7
|
1.0
|
|
O2G
|
D:ATP601
|
2.7
|
53.9
|
1.0
|
|
PB
|
D:ATP602
|
2.9
|
59.1
|
1.0
|
|
O1B
|
D:ATP602
|
3.0
|
60.4
|
1.0
|
|
HZ2
|
D:LYS210
|
3.1
|
77.3
|
1.0
|
|
PG
|
D:ATP602
|
3.1
|
64.5
|
1.0
|
|
O3A
|
D:ATP602
|
3.1
|
56.0
|
1.0
|
|
PB
|
D:ATP601
|
3.3
|
65.3
|
1.0
|
|
HZ3
|
D:LYS210
|
3.5
|
77.3
|
1.0
|
|
NZ
|
D:LYS210
|
3.7
|
64.3
|
1.0
|
|
O3B
|
D:ATP601
|
3.7
|
61.1
|
1.0
|
|
PG
|
D:ATP601
|
3.8
|
55.8
|
1.0
|
|
PA
|
D:ATP602
|
3.9
|
49.2
|
1.0
|
|
O3G
|
D:ATP602
|
4.0
|
63.5
|
1.0
|
|
O
|
D:HOH838
|
4.0
|
29.2
|
1.0
|
|
HE3
|
D:LYS210
|
4.0
|
75.6
|
1.0
|
|
O2A
|
D:ATP602
|
4.1
|
48.1
|
1.0
|
|
O2G
|
D:ATP602
|
4.1
|
64.5
|
1.0
|
|
HE22
|
G:GLN170
|
4.1
|
0.8
|
1.0
|
|
OE1
|
G:GLN170
|
4.2
|
92.4
|
1.0
|
|
O2B
|
D:ATP602
|
4.3
|
57.0
|
1.0
|
|
HZ1
|
D:LYS210
|
4.4
|
77.3
|
1.0
|
|
O1B
|
D:ATP601
|
4.4
|
63.5
|
1.0
|
|
CE
|
D:LYS210
|
4.5
|
62.9
|
1.0
|
|
O3A
|
D:ATP601
|
4.6
|
59.6
|
1.0
|
|
O2A
|
D:ATP601
|
4.6
|
50.0
|
1.0
|
|
O1G
|
D:ATP601
|
4.7
|
55.5
|
1.0
|
|
HZ
|
G:PHE171
|
4.7
|
0.2
|
1.0
|
|
O
|
D:HOH787
|
4.8
|
50.2
|
1.0
|
|
HG
|
D:SER166
|
4.8
|
0.2
|
1.0
|
|
NE2
|
G:GLN170
|
4.8
|
92.6
|
1.0
|
|
O1A
|
D:ATP602
|
4.8
|
49.4
|
1.0
|
|
HE2
|
D:LYS210
|
4.9
|
75.6
|
1.0
|
|
O3G
|
D:ATP601
|
4.9
|
56.4
|
1.0
|
|
CD
|
G:GLN170
|
4.9
|
92.6
|
1.0
|
|
PA
|
D:ATP601
|
4.9
|
51.5
|
1.0
|
|
HG23
|
D:THR227
|
5.0
|
93.3
|
1.0
|
|
Reference:
R.M.Buey,
D.Fernandez-Justel,
I.Marcos-Alcalde,
G.Winter,
P.Gomez-Puertas,
J.M.De Pereda,
J.Luis Revuelta.
A Nucleotide-Controlled Conformational Switch Modulates the Activity of Eukaryotic Imp Dehydrogenases. Sci Rep V. 7 2648 2017.
ISSN: ESSN 2045-2322
PubMed: 28572600
DOI: 10.1038/S41598-017-02805-X
Page generated: Mon Dec 14 20:51:09 2020
|
