Magnesium in PDB 7fry: Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
All present enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6:
2.7.1.40;
Protein crystallography data
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6, PDB code: 7fry
was solved by
A.Lulla,
O.Nilsson,
P.Brear,
A.Nain-Perez,
M.Grotli,
M.Hyvonen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
104.69 /
1.96
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
209.386,
113.888,
189.794,
90,
90.54,
90
|
R / Rfree (%)
|
20.1 /
22.3
|
Other elements in 7fry:
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
(pdb code 7fry). 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 Liver Pyruvate Kinase in Complex with Allosteric Modulator 6, PDB code: 7fry:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 1 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg603
b:49.0
occ:1.00
|
OD2
|
A:ASP308
|
2.0
|
69.9
|
1.0
|
OE2
|
A:GLU284
|
2.1
|
78.1
|
1.0
|
O1
|
A:OXL602
|
2.1
|
84.7
|
1.0
|
O2
|
A:OXL602
|
2.2
|
85.4
|
1.0
|
C1
|
A:OXL602
|
2.8
|
84.9
|
1.0
|
C2
|
A:OXL602
|
2.9
|
85.3
|
1.0
|
CD
|
A:GLU284
|
3.1
|
76.1
|
1.0
|
CG
|
A:ASP308
|
3.2
|
68.4
|
1.0
|
OE1
|
A:GLU284
|
3.5
|
78.1
|
1.0
|
CB
|
A:ASP308
|
3.8
|
63.4
|
1.0
|
O3
|
A:OXL602
|
4.1
|
84.5
|
1.0
|
O4
|
A:OXL602
|
4.1
|
85.2
|
1.0
|
NZ
|
A:LYS282
|
4.2
|
66.0
|
1.0
|
OD1
|
A:ASP308
|
4.2
|
69.8
|
1.0
|
CG
|
A:GLU284
|
4.5
|
69.1
|
1.0
|
CE
|
A:LYS282
|
4.5
|
64.8
|
1.0
|
N
|
A:ASP308
|
4.5
|
59.2
|
1.0
|
CE1
|
A:PHE256
|
4.6
|
73.8
|
1.0
|
CB
|
A:ALA305
|
4.7
|
52.2
|
1.0
|
CA
|
A:ASP308
|
4.8
|
60.9
|
1.0
|
CB
|
A:GLU284
|
4.9
|
64.1
|
1.0
|
CD1
|
A:PHE256
|
5.0
|
72.9
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 2 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg603
b:35.1
occ:1.00
|
O4
|
B:OXL602
|
1.9
|
65.7
|
1.0
|
OE2
|
B:GLU284
|
2.0
|
61.4
|
1.0
|
OD2
|
B:ASP308
|
2.0
|
55.6
|
1.0
|
O
|
B:HOH726
|
2.1
|
48.2
|
1.0
|
O3
|
B:OXL602
|
2.3
|
63.4
|
1.0
|
C2
|
B:OXL602
|
2.8
|
65.5
|
1.0
|
C1
|
B:OXL602
|
2.9
|
64.1
|
1.0
|
CD
|
B:GLU284
|
3.0
|
59.9
|
1.0
|
CG
|
B:ASP308
|
3.2
|
55.4
|
1.0
|
OE1
|
B:GLU284
|
3.4
|
63.5
|
1.0
|
CB
|
B:ASP308
|
3.7
|
49.0
|
1.0
|
O2
|
B:OXL602
|
4.0
|
66.3
|
1.0
|
O1
|
B:OXL602
|
4.1
|
63.5
|
1.0
|
NZ
|
B:LYS282
|
4.1
|
48.8
|
1.0
|
OD1
|
B:ASP308
|
4.2
|
58.5
|
1.0
|
CG
|
B:GLU284
|
4.4
|
52.2
|
1.0
|
CE
|
B:LYS282
|
4.4
|
48.4
|
1.0
|
N
|
B:ASP308
|
4.5
|
44.9
|
1.0
|
CE1
|
B:PHE256
|
4.6
|
62.3
|
1.0
|
CB
|
B:ALA305
|
4.6
|
42.4
|
1.0
|
CA
|
B:ASP308
|
4.7
|
46.2
|
1.0
|
CB
|
B:GLU284
|
4.9
|
48.5
|
1.0
|
CD1
|
B:PHE256
|
5.0
|
61.5
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 3 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg604
b:30.2
occ:1.00
|
OE2
|
C:GLU284
|
1.9
|
44.5
|
1.0
|
OD2
|
C:ASP308
|
2.0
|
57.3
|
1.0
|
O3
|
C:OXL603
|
2.1
|
57.4
|
1.0
|
O4
|
C:OXL603
|
2.2
|
57.9
|
1.0
|
O
|
C:HOH745
|
2.3
|
47.0
|
1.0
|
O
|
C:HOH735
|
2.3
|
47.7
|
1.0
|
C1
|
C:OXL603
|
2.9
|
57.7
|
1.0
|
C2
|
C:OXL603
|
3.0
|
57.8
|
1.0
|
CD
|
C:GLU284
|
3.0
|
45.5
|
1.0
|
CG
|
C:ASP308
|
3.2
|
56.0
|
1.0
|
OE1
|
C:GLU284
|
3.4
|
45.6
|
1.0
|
CB
|
C:ASP308
|
3.7
|
50.6
|
1.0
|
O1
|
C:OXL603
|
4.1
|
57.4
|
1.0
|
NZ
|
C:LYS282
|
4.2
|
41.5
|
1.0
|
O2
|
C:OXL603
|
4.2
|
57.7
|
1.0
|
OD1
|
C:ASP308
|
4.2
|
57.8
|
1.0
|
CG
|
C:GLU284
|
4.3
|
43.5
|
1.0
|
CE
|
C:LYS282
|
4.5
|
38.3
|
1.0
|
N
|
C:ASP308
|
4.5
|
47.5
|
1.0
|
CE1
|
C:PHE256
|
4.5
|
48.4
|
1.0
|
CB
|
C:ALA305
|
4.7
|
42.0
|
1.0
|
CA
|
C:ASP308
|
4.7
|
48.6
|
1.0
|
CB
|
C:GLU284
|
4.8
|
42.5
|
1.0
|
CD1
|
C:PHE256
|
4.9
|
47.3
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 4 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg603
b:22.8
occ:1.00
|
O
|
D:HOH736
|
2.0
|
41.1
|
1.0
|
OD2
|
D:ASP308
|
2.0
|
45.7
|
1.0
|
O2
|
D:OXL602
|
2.0
|
50.3
|
1.0
|
OE2
|
D:GLU284
|
2.1
|
38.4
|
1.0
|
O
|
D:HOH764
|
2.1
|
52.0
|
1.0
|
O1
|
D:OXL602
|
2.2
|
51.1
|
1.0
|
C2
|
D:OXL602
|
2.8
|
50.0
|
1.0
|
C1
|
D:OXL602
|
2.9
|
50.8
|
1.0
|
CD
|
D:GLU284
|
3.1
|
37.9
|
1.0
|
CG
|
D:ASP308
|
3.1
|
45.6
|
1.0
|
OE1
|
D:GLU284
|
3.5
|
35.6
|
1.0
|
CB
|
D:ASP308
|
3.7
|
39.8
|
1.0
|
O
|
D:HOH811
|
3.9
|
57.5
|
1.0
|
O4
|
D:OXL602
|
4.0
|
49.1
|
1.0
|
OD1
|
D:ASP308
|
4.2
|
47.5
|
1.0
|
NZ
|
D:LYS282
|
4.2
|
35.6
|
1.0
|
O3
|
D:OXL602
|
4.3
|
50.7
|
1.0
|
O
|
D:HOH802
|
4.3
|
40.5
|
1.0
|
N
|
D:ASP308
|
4.4
|
36.5
|
1.0
|
CG
|
D:GLU284
|
4.4
|
36.3
|
1.0
|
CE
|
D:LYS282
|
4.5
|
34.3
|
1.0
|
CB
|
D:ALA305
|
4.6
|
30.5
|
1.0
|
CE1
|
D:PHE256
|
4.7
|
47.0
|
1.0
|
CA
|
D:ASP308
|
4.7
|
37.8
|
1.0
|
CB
|
D:GLU284
|
4.9
|
34.3
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 5 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg603
b:42.8
occ:1.00
|
OD2
|
E:ASP308
|
1.9
|
63.5
|
1.0
|
O3
|
E:OXL602
|
1.9
|
82.0
|
1.0
|
OE2
|
E:GLU284
|
2.1
|
72.0
|
1.0
|
O4
|
E:OXL602
|
2.1
|
81.7
|
1.0
|
C1
|
E:OXL602
|
2.7
|
81.9
|
1.0
|
C2
|
E:OXL602
|
2.8
|
81.8
|
1.0
|
CG
|
E:ASP308
|
3.1
|
61.6
|
1.0
|
CD
|
E:GLU284
|
3.1
|
70.5
|
1.0
|
OE1
|
E:GLU284
|
3.6
|
71.8
|
1.0
|
CB
|
E:ASP308
|
3.6
|
57.3
|
1.0
|
O2
|
E:OXL602
|
4.0
|
82.0
|
1.0
|
O1
|
E:OXL602
|
4.0
|
81.8
|
1.0
|
OD1
|
E:ASP308
|
4.1
|
61.9
|
1.0
|
N
|
E:ASP308
|
4.3
|
54.7
|
1.0
|
NZ
|
E:LYS282
|
4.3
|
59.4
|
1.0
|
O
|
E:HOH825
|
4.3
|
71.8
|
1.0
|
CG
|
E:GLU284
|
4.4
|
63.3
|
1.0
|
CA
|
E:ASP308
|
4.6
|
55.5
|
1.0
|
CE
|
E:LYS282
|
4.6
|
59.0
|
1.0
|
CE1
|
E:PHE256
|
4.6
|
69.8
|
1.0
|
CB
|
E:ALA305
|
4.7
|
51.0
|
1.0
|
CB
|
E:GLU284
|
4.9
|
58.4
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 6 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg603
b:35.0
occ:1.00
|
OE2
|
F:GLU284
|
2.0
|
53.5
|
1.0
|
OD2
|
F:ASP308
|
2.0
|
55.6
|
1.0
|
O
|
F:HOH707
|
2.1
|
49.1
|
1.0
|
O1
|
F:OXL602
|
2.1
|
75.0
|
1.0
|
O2
|
F:OXL602
|
2.4
|
76.3
|
1.0
|
C1
|
F:OXL602
|
3.0
|
75.2
|
1.0
|
CD
|
F:GLU284
|
3.0
|
54.2
|
1.0
|
C2
|
F:OXL602
|
3.1
|
75.8
|
1.0
|
CG
|
F:ASP308
|
3.1
|
54.0
|
1.0
|
OE1
|
F:GLU284
|
3.4
|
55.6
|
1.0
|
CB
|
F:ASP308
|
3.7
|
46.6
|
1.0
|
O
|
F:HOH828
|
4.0
|
59.7
|
1.0
|
O3
|
F:OXL602
|
4.1
|
74.8
|
1.0
|
NZ
|
F:LYS282
|
4.1
|
49.6
|
1.0
|
OD1
|
F:ASP308
|
4.2
|
57.6
|
1.0
|
O4
|
F:OXL602
|
4.3
|
75.9
|
1.0
|
CG
|
F:GLU284
|
4.3
|
48.6
|
1.0
|
CE
|
F:LYS282
|
4.4
|
47.0
|
1.0
|
N
|
F:ASP308
|
4.5
|
42.1
|
1.0
|
CE1
|
F:PHE256
|
4.6
|
54.6
|
1.0
|
CB
|
F:ALA305
|
4.6
|
37.4
|
1.0
|
CA
|
F:ASP308
|
4.7
|
43.7
|
1.0
|
CB
|
F:GLU284
|
4.8
|
45.0
|
1.0
|
CD1
|
F:PHE256
|
5.0
|
53.6
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 7 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg603
b:23.7
occ:1.00
|
OE2
|
G:GLU284
|
2.0
|
40.7
|
1.0
|
OD2
|
G:ASP308
|
2.0
|
53.3
|
1.0
|
O2
|
G:OXL602
|
2.0
|
53.0
|
1.0
|
O1
|
G:OXL602
|
2.1
|
53.1
|
1.0
|
O
|
G:HOH739
|
2.1
|
44.2
|
1.0
|
O
|
G:HOH721
|
2.1
|
42.0
|
1.0
|
C2
|
G:OXL602
|
2.7
|
53.2
|
1.0
|
C1
|
G:OXL602
|
2.8
|
52.9
|
1.0
|
CD
|
G:GLU284
|
3.0
|
40.1
|
1.0
|
CG
|
G:ASP308
|
3.1
|
52.5
|
1.0
|
OE1
|
G:GLU284
|
3.4
|
40.4
|
1.0
|
CB
|
G:ASP308
|
3.7
|
45.3
|
1.0
|
O3
|
G:OXL602
|
4.0
|
52.3
|
1.0
|
O4
|
G:OXL602
|
4.0
|
53.7
|
1.0
|
O
|
G:HOH848
|
4.0
|
54.9
|
1.0
|
NZ
|
G:LYS282
|
4.2
|
33.9
|
1.0
|
OD1
|
G:ASP308
|
4.2
|
55.9
|
1.0
|
CG
|
G:GLU284
|
4.4
|
37.4
|
1.0
|
O
|
G:HOH754
|
4.4
|
48.3
|
1.0
|
N
|
G:ASP308
|
4.4
|
41.4
|
1.0
|
CE
|
G:LYS282
|
4.5
|
32.1
|
1.0
|
CE1
|
G:PHE256
|
4.6
|
44.6
|
1.0
|
CB
|
G:ALA305
|
4.6
|
35.1
|
1.0
|
CA
|
G:ASP308
|
4.7
|
42.6
|
1.0
|
CB
|
G:GLU284
|
4.8
|
35.3
|
1.0
|
CD1
|
G:PHE256
|
5.0
|
43.2
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 7fry
Go back to
Magnesium Binding Sites List in 7fry
Magnesium binding site 8 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 6 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg603
b:21.9
occ:1.00
|
O4
|
H:OXL602
|
1.9
|
45.3
|
1.0
|
O
|
H:HOH712
|
1.9
|
43.8
|
1.0
|
OD2
|
H:ASP308
|
2.0
|
44.9
|
1.0
|
OE2
|
H:GLU284
|
2.0
|
41.3
|
1.0
|
O
|
H:HOH738
|
2.1
|
31.2
|
1.0
|
O3
|
H:OXL602
|
2.1
|
44.1
|
1.0
|
C2
|
H:OXL602
|
2.7
|
45.6
|
1.0
|
C1
|
H:OXL602
|
2.9
|
45.2
|
1.0
|
CD
|
H:GLU284
|
3.0
|
40.1
|
1.0
|
CG
|
H:ASP308
|
3.1
|
44.0
|
1.0
|
OE1
|
H:GLU284
|
3.5
|
40.9
|
1.0
|
CB
|
H:ASP308
|
3.7
|
37.8
|
1.0
|
O2
|
H:OXL602
|
4.0
|
46.1
|
1.0
|
O1
|
H:OXL602
|
4.1
|
45.6
|
1.0
|
NZ
|
H:LYS282
|
4.2
|
40.4
|
1.0
|
OD1
|
H:ASP308
|
4.2
|
46.8
|
1.0
|
O
|
H:HOH889
|
4.2
|
50.4
|
1.0
|
N
|
H:ASP308
|
4.3
|
35.1
|
1.0
|
CG
|
H:GLU284
|
4.3
|
36.5
|
1.0
|
CE
|
H:LYS282
|
4.4
|
37.1
|
1.0
|
O
|
H:HOH930
|
4.6
|
79.4
|
1.0
|
CB
|
H:ALA305
|
4.6
|
29.7
|
1.0
|
CA
|
H:ASP308
|
4.6
|
36.2
|
1.0
|
CE1
|
H:PHE256
|
4.6
|
43.5
|
1.0
|
CB
|
H:GLU284
|
4.8
|
35.2
|
1.0
|
|
Reference:
A.Nain-Perez,
O.Nilsson,
A.Lulla,
L.Haversen,
P.Brear,
S.Liljenberg,
M.Hyvonen,
J.Boren,
M.Grotli.
Tuning Liver Pyruvate Kinase Activity Up or Down with A New Class of Allosteric Modulators. Eur.J.Med.Chem. V. 250 15177 2023.
ISSN: ISSN 0223-5234
PubMed: 36753880
DOI: 10.1016/J.EJMECH.2023.115177
Page generated: Wed Oct 2 21:36:57 2024
|