Potassium in PDB 7frv: Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
All present enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3:
2.7.1.40;
Protein crystallography data
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3, PDB code: 7frv
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)
|
188.34 /
2.00
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
208.043,
112.707,
188.415,
90,
91.59,
90
|
R / Rfree (%)
|
20.6 /
23.2
|
Other elements in 7frv:
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
(pdb code 7frv). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3, PDB code: 7frv:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 1 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K604
b:84.0
occ:1.00
|
OD1
|
A:ASN87
|
2.5
|
68.0
|
1.0
|
O
|
A:THR126
|
2.7
|
68.6
|
1.0
|
OD1
|
A:ASP125
|
2.7
|
66.1
|
1.0
|
OG
|
A:SER89
|
2.8
|
77.3
|
1.0
|
C
|
A:THR126
|
3.6
|
68.7
|
1.0
|
CG
|
A:ASN87
|
3.7
|
67.7
|
1.0
|
CG
|
A:ASP125
|
3.7
|
65.4
|
1.0
|
O
|
A:ASP125
|
3.7
|
61.4
|
1.0
|
CB
|
A:SER89
|
3.8
|
75.2
|
1.0
|
OG
|
A:SER255
|
3.9
|
63.0
|
1.0
|
N
|
A:SER89
|
4.1
|
72.4
|
1.0
|
C
|
A:ASP125
|
4.1
|
61.7
|
1.0
|
NZ
|
A:LYS282
|
4.1
|
63.5
|
1.0
|
CA
|
A:LYS127
|
4.2
|
72.8
|
1.0
|
N
|
A:LYS127
|
4.2
|
70.6
|
1.0
|
CB
|
A:ASP125
|
4.2
|
61.3
|
1.0
|
NH2
|
A:ARG85
|
4.2
|
59.6
|
1.0
|
ND2
|
A:ASN87
|
4.3
|
68.7
|
1.0
|
N
|
A:THR126
|
4.5
|
63.5
|
1.0
|
CA
|
A:SER89
|
4.5
|
74.0
|
1.0
|
OD2
|
A:ASP125
|
4.6
|
66.9
|
1.0
|
N
|
A:PHE88
|
4.6
|
68.2
|
1.0
|
CA
|
A:THR126
|
4.6
|
65.9
|
1.0
|
O
|
A:LYS127
|
4.6
|
74.5
|
1.0
|
C
|
A:LYS127
|
4.7
|
74.5
|
1.0
|
CB
|
A:ASN87
|
4.8
|
65.5
|
1.0
|
CA
|
A:ASP125
|
4.8
|
59.9
|
1.0
|
CA
|
A:ASN87
|
4.8
|
64.8
|
1.0
|
O2
|
A:OXL602
|
4.9
|
85.9
|
1.0
|
C
|
A:ASN87
|
4.9
|
67.1
|
1.0
|
C
|
A:PHE88
|
4.9
|
71.4
|
1.0
|
|
Potassium binding site 2 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 2 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K604
b:73.9
occ:1.00
|
O
|
B:HOH811
|
2.4
|
57.2
|
1.0
|
OD1
|
B:ASN87
|
2.5
|
64.8
|
1.0
|
OD1
|
B:ASP125
|
2.7
|
69.4
|
1.0
|
O
|
B:THR126
|
2.8
|
72.8
|
1.0
|
OG
|
B:SER89
|
2.8
|
78.2
|
1.0
|
O
|
B:HOH779
|
3.6
|
106.4
|
1.0
|
O
|
B:HOH840
|
3.6
|
65.0
|
1.0
|
CG
|
B:ASN87
|
3.6
|
65.5
|
1.0
|
CG
|
B:ASP125
|
3.6
|
70.3
|
1.0
|
C
|
B:THR126
|
3.7
|
72.7
|
1.0
|
O
|
B:ASP125
|
3.7
|
66.8
|
1.0
|
CB
|
B:SER89
|
3.8
|
76.0
|
1.0
|
OG
|
B:SER255
|
4.0
|
54.5
|
1.0
|
N
|
B:SER89
|
4.1
|
73.2
|
1.0
|
NZ
|
B:LYS282
|
4.1
|
61.5
|
1.0
|
C
|
B:ASP125
|
4.1
|
66.6
|
1.0
|
NH2
|
B:ARG85
|
4.2
|
57.3
|
1.0
|
ND2
|
B:ASN87
|
4.2
|
67.2
|
1.0
|
CB
|
B:ASP125
|
4.2
|
66.1
|
1.0
|
CA
|
B:LYS127
|
4.3
|
76.6
|
1.0
|
N
|
B:LYS127
|
4.3
|
74.5
|
1.0
|
N
|
B:THR126
|
4.5
|
67.9
|
1.0
|
CA
|
B:SER89
|
4.5
|
74.8
|
1.0
|
OD2
|
B:ASP125
|
4.5
|
73.7
|
1.0
|
N
|
B:PHE88
|
4.6
|
67.9
|
1.0
|
CA
|
B:THR126
|
4.6
|
70.1
|
1.0
|
O
|
B:LYS127
|
4.7
|
78.2
|
1.0
|
CB
|
B:ASN87
|
4.7
|
64.1
|
1.0
|
C
|
B:LYS127
|
4.8
|
78.3
|
1.0
|
CA
|
B:ASN87
|
4.8
|
64.0
|
1.0
|
CA
|
B:ASP125
|
4.8
|
64.8
|
1.0
|
C
|
B:ASN87
|
4.9
|
66.2
|
1.0
|
C
|
B:PHE88
|
5.0
|
72.1
|
1.0
|
|
Potassium binding site 3 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 3 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K604
b:56.4
occ:1.00
|
OD1
|
C:ASN87
|
2.4
|
45.0
|
1.0
|
OD1
|
C:ASP125
|
2.7
|
44.0
|
1.0
|
OG
|
C:SER89
|
2.8
|
46.0
|
1.0
|
O
|
C:THR126
|
2.8
|
39.5
|
1.0
|
O
|
C:HOH839
|
3.2
|
49.2
|
1.0
|
O
|
C:HOH759
|
3.4
|
84.5
|
1.0
|
CG
|
C:ASN87
|
3.5
|
44.4
|
1.0
|
O
|
C:ASP125
|
3.6
|
39.3
|
1.0
|
CG
|
C:ASP125
|
3.6
|
44.1
|
1.0
|
C
|
C:THR126
|
3.6
|
40.6
|
1.0
|
CB
|
C:SER89
|
3.7
|
43.9
|
1.0
|
N
|
C:SER89
|
3.9
|
42.4
|
1.0
|
C
|
C:ASP125
|
4.0
|
38.9
|
1.0
|
OG
|
C:SER255
|
4.1
|
41.4
|
1.0
|
CB
|
C:ASP125
|
4.1
|
39.1
|
1.0
|
ND2
|
C:ASN87
|
4.2
|
44.9
|
1.0
|
NH2
|
C:ARG85
|
4.2
|
47.0
|
1.0
|
NZ
|
C:LYS282
|
4.2
|
48.2
|
1.0
|
N
|
C:LYS127
|
4.3
|
42.1
|
1.0
|
CA
|
C:LYS127
|
4.3
|
43.8
|
1.0
|
CA
|
C:SER89
|
4.4
|
44.0
|
1.0
|
N
|
C:PHE88
|
4.4
|
39.9
|
1.0
|
N
|
C:THR126
|
4.4
|
39.1
|
1.0
|
OD2
|
C:ASP125
|
4.5
|
47.5
|
1.0
|
CA
|
C:THR126
|
4.6
|
39.6
|
1.0
|
CB
|
C:ASN87
|
4.6
|
41.8
|
1.0
|
CA
|
C:ASN87
|
4.6
|
40.6
|
1.0
|
O
|
C:HOH889
|
4.6
|
62.9
|
1.0
|
C
|
C:ASN87
|
4.7
|
40.5
|
1.0
|
CA
|
C:ASP125
|
4.7
|
37.6
|
1.0
|
O
|
C:LYS127
|
4.8
|
45.2
|
1.0
|
C
|
C:PHE88
|
4.8
|
41.5
|
1.0
|
C
|
C:LYS127
|
4.9
|
44.7
|
1.0
|
|
Potassium binding site 4 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 4 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K604
b:45.9
occ:1.00
|
OD1
|
D:ASN87
|
2.6
|
34.5
|
1.0
|
OD1
|
D:ASP125
|
2.7
|
33.5
|
1.0
|
O
|
D:THR126
|
2.7
|
36.2
|
1.0
|
OG
|
D:SER89
|
2.8
|
36.4
|
1.0
|
O
|
D:HOH778
|
2.9
|
36.9
|
1.0
|
C
|
D:THR126
|
3.6
|
36.3
|
1.0
|
CG
|
D:ASP125
|
3.6
|
33.9
|
1.0
|
CG
|
D:ASN87
|
3.7
|
32.3
|
1.0
|
O
|
D:HOH958
|
3.8
|
65.8
|
1.0
|
O
|
D:ASP125
|
3.8
|
31.6
|
1.0
|
OG
|
D:SER255
|
3.8
|
37.9
|
1.0
|
CB
|
D:SER89
|
3.8
|
33.3
|
1.0
|
NZ
|
D:LYS282
|
4.0
|
33.1
|
1.0
|
C
|
D:ASP125
|
4.1
|
31.4
|
1.0
|
N
|
D:SER89
|
4.1
|
31.7
|
1.0
|
CA
|
D:LYS127
|
4.2
|
41.5
|
1.0
|
ND2
|
D:ASN87
|
4.2
|
31.6
|
1.0
|
N
|
D:LYS127
|
4.2
|
38.6
|
1.0
|
NH2
|
D:ARG85
|
4.3
|
32.4
|
1.0
|
CB
|
D:ASP125
|
4.3
|
29.5
|
1.0
|
N
|
D:THR126
|
4.4
|
31.6
|
1.0
|
OD2
|
D:ASP125
|
4.5
|
36.1
|
1.0
|
CA
|
D:SER89
|
4.5
|
32.6
|
1.0
|
O
|
D:LYS127
|
4.6
|
44.9
|
1.0
|
CA
|
D:THR126
|
4.6
|
33.0
|
1.0
|
N
|
D:PHE88
|
4.7
|
30.1
|
1.0
|
C
|
D:LYS127
|
4.7
|
44.6
|
1.0
|
CA
|
D:ASP125
|
4.8
|
29.4
|
1.0
|
CB
|
D:ASN87
|
4.9
|
29.3
|
1.0
|
CA
|
D:ASN87
|
4.9
|
28.5
|
1.0
|
C
|
D:ASN87
|
5.0
|
29.3
|
1.0
|
|
Potassium binding site 5 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 5 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K604
b:83.1
occ:1.00
|
OD1
|
E:ASP125
|
2.6
|
62.9
|
1.0
|
O
|
E:THR126
|
2.6
|
66.2
|
1.0
|
OD1
|
E:ASN87
|
2.6
|
60.7
|
1.0
|
OG
|
E:SER89
|
2.9
|
72.2
|
1.0
|
C
|
E:THR126
|
3.5
|
66.1
|
1.0
|
CG
|
E:ASP125
|
3.6
|
62.9
|
1.0
|
O
|
E:ASP125
|
3.6
|
60.5
|
1.0
|
CG
|
E:ASN87
|
3.8
|
59.5
|
1.0
|
OG
|
E:SER255
|
3.8
|
57.0
|
1.0
|
CB
|
E:SER89
|
3.9
|
69.5
|
1.0
|
C
|
E:ASP125
|
3.9
|
60.5
|
1.0
|
NZ
|
E:LYS282
|
4.0
|
53.5
|
1.0
|
N
|
E:SER89
|
4.1
|
66.2
|
1.0
|
CB
|
E:ASP125
|
4.1
|
59.9
|
1.0
|
N
|
E:LYS127
|
4.2
|
67.9
|
1.0
|
CA
|
E:LYS127
|
4.2
|
70.1
|
1.0
|
NH2
|
E:ARG85
|
4.3
|
50.5
|
1.0
|
N
|
E:THR126
|
4.3
|
61.8
|
1.0
|
ND2
|
E:ASN87
|
4.4
|
59.9
|
1.0
|
OD2
|
E:ASP125
|
4.5
|
64.6
|
1.0
|
CA
|
E:THR126
|
4.5
|
63.7
|
1.0
|
CA
|
E:SER89
|
4.6
|
68.0
|
1.0
|
N
|
E:PHE88
|
4.6
|
60.4
|
1.0
|
O
|
E:LYS127
|
4.6
|
72.4
|
1.0
|
CA
|
E:ASP125
|
4.7
|
59.0
|
1.0
|
C
|
E:LYS127
|
4.7
|
72.0
|
1.0
|
CA
|
E:ASN87
|
4.8
|
56.7
|
1.0
|
CB
|
E:ASN87
|
4.8
|
56.9
|
1.0
|
C
|
E:ASN87
|
4.9
|
58.8
|
1.0
|
C
|
E:PHE88
|
5.0
|
65.0
|
1.0
|
|
Potassium binding site 6 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 6 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K604
b:71.2
occ:1.00
|
OD1
|
F:ASN87
|
2.5
|
44.4
|
1.0
|
OD1
|
F:ASP125
|
2.6
|
52.0
|
1.0
|
O
|
F:THR126
|
2.7
|
49.0
|
1.0
|
OG
|
F:SER89
|
2.9
|
58.3
|
1.0
|
O
|
F:HOH730
|
3.0
|
68.4
|
1.0
|
O
|
F:HOH892
|
3.0
|
56.9
|
1.0
|
CG
|
F:ASP125
|
3.6
|
50.2
|
1.0
|
C
|
F:THR126
|
3.6
|
49.5
|
1.0
|
O
|
F:ASP125
|
3.6
|
41.9
|
1.0
|
CG
|
F:ASN87
|
3.7
|
44.9
|
1.0
|
O
|
F:HOH887
|
3.7
|
54.9
|
1.0
|
CB
|
F:SER89
|
3.9
|
56.9
|
1.0
|
OG
|
F:SER255
|
4.0
|
43.2
|
1.0
|
C
|
F:ASP125
|
4.0
|
43.0
|
1.0
|
NZ
|
F:LYS282
|
4.0
|
39.8
|
1.0
|
N
|
F:SER89
|
4.1
|
54.9
|
1.0
|
CB
|
F:ASP125
|
4.1
|
43.5
|
1.0
|
NH2
|
F:ARG85
|
4.1
|
44.0
|
1.0
|
N
|
F:LYS127
|
4.3
|
51.4
|
1.0
|
CA
|
F:LYS127
|
4.3
|
54.2
|
1.0
|
ND2
|
F:ASN87
|
4.3
|
47.1
|
1.0
|
N
|
F:THR126
|
4.4
|
45.1
|
1.0
|
OD2
|
F:ASP125
|
4.4
|
52.1
|
1.0
|
CA
|
F:SER89
|
4.5
|
56.4
|
1.0
|
N
|
F:PHE88
|
4.6
|
47.9
|
1.0
|
CA
|
F:THR126
|
4.6
|
47.3
|
1.0
|
CA
|
F:ASP125
|
4.7
|
41.8
|
1.0
|
O
|
F:LYS127
|
4.7
|
56.8
|
1.0
|
CB
|
F:ASN87
|
4.8
|
42.4
|
1.0
|
CA
|
F:ASN87
|
4.8
|
42.7
|
1.0
|
C
|
F:LYS127
|
4.8
|
56.7
|
1.0
|
C
|
F:ASN87
|
4.9
|
45.8
|
1.0
|
C
|
F:PHE88
|
5.0
|
53.8
|
1.0
|
|
Potassium binding site 7 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 7 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K605
b:54.9
occ:1.00
|
O
|
G:THR126
|
2.6
|
36.0
|
1.0
|
OD1
|
G:ASP125
|
2.7
|
41.0
|
1.0
|
OD1
|
G:ASN87
|
2.7
|
36.9
|
1.0
|
OG
|
G:SER89
|
2.8
|
42.7
|
1.0
|
C
|
G:THR126
|
3.5
|
37.1
|
1.0
|
CG
|
G:ASP125
|
3.7
|
39.5
|
1.0
|
OG
|
G:SER255
|
3.7
|
39.6
|
1.0
|
O
|
G:ASP125
|
3.8
|
32.9
|
1.0
|
CG
|
G:ASN87
|
3.9
|
35.7
|
1.0
|
CB
|
G:SER89
|
3.9
|
40.8
|
1.0
|
NZ
|
G:LYS282
|
4.0
|
37.6
|
1.0
|
C
|
G:ASP125
|
4.1
|
32.8
|
1.0
|
O
|
G:HOH978
|
4.1
|
76.2
|
1.0
|
CA
|
G:LYS127
|
4.1
|
41.5
|
1.0
|
N
|
G:LYS127
|
4.1
|
39.3
|
1.0
|
N
|
G:SER89
|
4.2
|
39.4
|
1.0
|
CB
|
G:ASP125
|
4.3
|
33.4
|
1.0
|
NH2
|
G:ARG85
|
4.3
|
42.7
|
1.0
|
N
|
G:THR126
|
4.4
|
33.5
|
1.0
|
ND2
|
G:ASN87
|
4.4
|
36.0
|
1.0
|
O
|
G:LYS127
|
4.5
|
42.5
|
1.0
|
CA
|
G:THR126
|
4.5
|
34.9
|
1.0
|
OD2
|
G:ASP125
|
4.5
|
42.7
|
1.0
|
CA
|
G:SER89
|
4.6
|
40.5
|
1.0
|
C
|
G:LYS127
|
4.6
|
42.2
|
1.0
|
O
|
G:HOH750
|
4.7
|
48.4
|
1.0
|
N
|
G:PHE88
|
4.7
|
36.1
|
1.0
|
CA
|
G:ASP125
|
4.8
|
31.4
|
1.0
|
CB
|
G:SER255
|
4.9
|
37.3
|
1.0
|
CB
|
G:ASN87
|
5.0
|
33.7
|
1.0
|
CA
|
G:ASN87
|
5.0
|
33.8
|
1.0
|
|
Potassium binding site 8 out
of 8 in 7frv
Go back to
Potassium Binding Sites List in 7frv
Potassium binding site 8 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 3 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K604
b:47.9
occ:1.00
|
OD1
|
H:ASN87
|
2.6
|
27.9
|
1.0
|
OD1
|
H:ASP125
|
2.6
|
32.2
|
1.0
|
O
|
H:THR126
|
2.7
|
30.9
|
1.0
|
O
|
H:HOH885
|
2.9
|
40.6
|
1.0
|
OG
|
H:SER89
|
2.9
|
38.4
|
1.0
|
CG
|
H:ASP125
|
3.6
|
32.2
|
1.0
|
C
|
H:THR126
|
3.6
|
31.8
|
1.0
|
CG
|
H:ASN87
|
3.7
|
28.4
|
1.0
|
O
|
H:ASP125
|
3.8
|
28.5
|
1.0
|
OG
|
H:SER255
|
3.8
|
30.7
|
1.0
|
NZ
|
H:LYS282
|
3.9
|
34.7
|
1.0
|
CB
|
H:SER89
|
3.9
|
34.8
|
1.0
|
C
|
H:ASP125
|
4.1
|
28.4
|
1.0
|
NH2
|
H:ARG85
|
4.2
|
32.7
|
1.0
|
N
|
H:SER89
|
4.2
|
32.6
|
1.0
|
CB
|
H:ASP125
|
4.2
|
27.5
|
1.0
|
ND2
|
H:ASN87
|
4.2
|
28.0
|
1.0
|
O
|
H:HOH967
|
4.2
|
58.5
|
1.0
|
N
|
H:LYS127
|
4.3
|
34.3
|
1.0
|
CA
|
H:LYS127
|
4.3
|
37.7
|
1.0
|
N
|
H:THR126
|
4.4
|
29.1
|
1.0
|
OD2
|
H:ASP125
|
4.4
|
35.5
|
1.0
|
CA
|
H:THR126
|
4.6
|
30.2
|
1.0
|
CA
|
H:SER89
|
4.6
|
34.0
|
1.0
|
O
|
H:LYS127
|
4.7
|
40.2
|
1.0
|
N
|
H:PHE88
|
4.7
|
28.0
|
1.0
|
C
|
H:LYS127
|
4.8
|
40.4
|
1.0
|
CA
|
H:ASP125
|
4.8
|
26.7
|
1.0
|
O
|
H:HOH747
|
4.8
|
35.7
|
1.0
|
CB
|
H:ASN87
|
4.8
|
26.0
|
1.0
|
O3
|
H:OXL602
|
4.8
|
51.5
|
1.0
|
CA
|
H:ASN87
|
4.9
|
25.8
|
1.0
|
C
|
H:ASN87
|
5.0
|
27.4
|
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: Mon Aug 12 18:55:50 2024
|