Potassium in PDB 7fsc: Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
Enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
All present enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42:
2.7.1.40;
Protein crystallography data
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42, PDB code: 7fsc
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)
|
104.56 /
1.86
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
209.159,
113.004,
189.435,
90,
91.14,
90
|
R / Rfree (%)
|
19.8 /
22.2
|
Other elements in 7fsc:
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42 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 42
(pdb code 7fsc). 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 42, PDB code: 7fsc:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 1 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K604
b:62.3
occ:1.00
|
OD1
|
A:ASN87
|
2.5
|
49.9
|
1.0
|
OG
|
A:SER89
|
2.7
|
56.6
|
1.0
|
OD1
|
A:ASP125
|
2.7
|
44.9
|
1.0
|
O
|
A:THR126
|
2.9
|
48.2
|
1.0
|
O
|
A:HOH854
|
3.0
|
65.4
|
1.0
|
CG
|
A:ASN87
|
3.6
|
49.0
|
1.0
|
CG
|
A:ASP125
|
3.6
|
45.1
|
1.0
|
C
|
A:THR126
|
3.7
|
48.9
|
1.0
|
CB
|
A:SER89
|
3.8
|
54.2
|
1.0
|
O
|
A:ASP125
|
3.8
|
43.9
|
1.0
|
OG
|
A:SER255
|
3.9
|
45.5
|
1.0
|
N
|
A:SER89
|
4.1
|
51.5
|
1.0
|
NZ
|
A:LYS282
|
4.1
|
44.5
|
1.0
|
C
|
A:ASP125
|
4.2
|
44.2
|
1.0
|
NH2
|
A:ARG85
|
4.2
|
41.7
|
1.0
|
ND2
|
A:ASN87
|
4.2
|
49.4
|
1.0
|
CA
|
A:LYS127
|
4.3
|
52.1
|
1.0
|
CB
|
A:ASP125
|
4.3
|
42.9
|
1.0
|
N
|
A:LYS127
|
4.3
|
50.2
|
1.0
|
OD2
|
A:ASP125
|
4.4
|
47.4
|
1.0
|
CA
|
A:SER89
|
4.5
|
53.0
|
1.0
|
N
|
A:THR126
|
4.6
|
45.8
|
1.0
|
N
|
A:PHE88
|
4.6
|
47.6
|
1.0
|
O
|
A:HOH736
|
4.7
|
38.4
|
1.0
|
O
|
A:LYS127
|
4.7
|
54.4
|
1.0
|
CA
|
A:THR126
|
4.7
|
47.3
|
1.0
|
CB
|
A:ASN87
|
4.7
|
46.2
|
1.0
|
C
|
A:LYS127
|
4.8
|
54.2
|
1.0
|
CA
|
A:ASN87
|
4.8
|
45.4
|
1.0
|
CA
|
A:ASP125
|
4.9
|
42.5
|
1.0
|
C
|
A:ASN87
|
4.9
|
46.9
|
1.0
|
C
|
A:PHE88
|
5.0
|
50.5
|
1.0
|
|
Potassium binding site 2 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 2 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K604
b:60.8
occ:1.00
|
OD1
|
B:ASN87
|
2.6
|
41.7
|
1.0
|
OD1
|
B:ASP125
|
2.7
|
42.4
|
1.0
|
O
|
B:HOH852
|
2.8
|
54.6
|
1.0
|
OG
|
B:SER89
|
2.8
|
54.7
|
1.0
|
O
|
B:THR126
|
2.9
|
45.1
|
1.0
|
O
|
B:HOH933
|
3.1
|
63.9
|
1.0
|
CG
|
B:ASP125
|
3.6
|
42.2
|
1.0
|
CG
|
B:ASN87
|
3.7
|
41.7
|
1.0
|
C
|
B:THR126
|
3.7
|
45.4
|
1.0
|
OG
|
B:SER255
|
3.8
|
39.2
|
1.0
|
O
|
B:ASP125
|
3.9
|
39.8
|
1.0
|
CB
|
B:SER89
|
3.9
|
51.9
|
1.0
|
NZ
|
B:LYS282
|
3.9
|
35.7
|
1.0
|
NH2
|
B:ARG85
|
4.2
|
36.8
|
1.0
|
C
|
B:ASP125
|
4.2
|
39.5
|
1.0
|
N
|
B:SER89
|
4.2
|
48.9
|
1.0
|
CB
|
B:ASP125
|
4.3
|
38.4
|
1.0
|
ND2
|
B:ASN87
|
4.3
|
42.9
|
1.0
|
CA
|
B:LYS127
|
4.3
|
49.6
|
1.0
|
OD2
|
B:ASP125
|
4.4
|
43.6
|
1.0
|
N
|
B:LYS127
|
4.4
|
47.3
|
1.0
|
N
|
B:THR126
|
4.6
|
40.8
|
1.0
|
CA
|
B:SER89
|
4.6
|
50.4
|
1.0
|
O
|
B:LYS127
|
4.7
|
51.3
|
1.0
|
CA
|
B:THR126
|
4.7
|
42.8
|
1.0
|
N
|
B:PHE88
|
4.8
|
43.1
|
1.0
|
C
|
B:LYS127
|
4.8
|
51.3
|
1.0
|
CB
|
B:ASN87
|
4.8
|
39.9
|
1.0
|
CA
|
B:ASP125
|
4.9
|
37.7
|
1.0
|
CA
|
B:ASN87
|
4.9
|
39.6
|
1.0
|
O
|
B:HOH919
|
4.9
|
54.9
|
1.0
|
|
Potassium binding site 3 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 3 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K604
b:52.6
occ:1.00
|
OD1
|
C:ASN87
|
2.5
|
32.9
|
1.0
|
OD1
|
C:ASP125
|
2.6
|
33.0
|
1.0
|
OG
|
C:SER89
|
2.8
|
36.5
|
1.0
|
O
|
C:THR126
|
2.9
|
27.4
|
1.0
|
O
|
C:HOH891
|
3.0
|
36.9
|
1.0
|
CG
|
C:ASP125
|
3.5
|
31.6
|
1.0
|
CG
|
C:ASN87
|
3.6
|
32.5
|
1.0
|
C
|
C:THR126
|
3.7
|
28.0
|
1.0
|
O
|
C:ASP125
|
3.8
|
25.9
|
1.0
|
CB
|
C:SER89
|
3.9
|
34.5
|
1.0
|
OG
|
C:SER255
|
3.9
|
28.3
|
1.0
|
NZ
|
C:LYS282
|
4.0
|
27.8
|
1.0
|
C
|
C:ASP125
|
4.1
|
26.1
|
1.0
|
N
|
C:SER89
|
4.1
|
32.4
|
1.0
|
NH2
|
C:ARG85
|
4.1
|
34.2
|
1.0
|
CB
|
C:ASP125
|
4.2
|
26.7
|
1.0
|
ND2
|
C:ASN87
|
4.2
|
32.7
|
1.0
|
CA
|
C:LYS127
|
4.3
|
31.4
|
1.0
|
N
|
C:LYS127
|
4.3
|
29.4
|
1.0
|
OD2
|
C:ASP125
|
4.3
|
33.1
|
1.0
|
O
|
C:HOH907
|
4.4
|
48.0
|
1.0
|
N
|
C:THR126
|
4.5
|
26.4
|
1.0
|
CA
|
C:SER89
|
4.5
|
33.9
|
1.0
|
N
|
C:PHE88
|
4.6
|
28.2
|
1.0
|
CA
|
C:THR126
|
4.7
|
26.7
|
1.0
|
O
|
C:LYS127
|
4.7
|
33.3
|
1.0
|
CB
|
C:ASN87
|
4.7
|
29.4
|
1.0
|
CA
|
C:ASP125
|
4.8
|
25.6
|
1.0
|
O
|
C:HOH743
|
4.8
|
27.6
|
1.0
|
CA
|
C:ASN87
|
4.8
|
28.1
|
1.0
|
C
|
C:LYS127
|
4.8
|
32.9
|
1.0
|
O
|
C:HOH964
|
4.9
|
73.6
|
1.0
|
C
|
C:ASN87
|
4.9
|
28.2
|
1.0
|
|
Potassium binding site 4 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 4 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K604
b:47.8
occ:1.00
|
OD1
|
D:ASN87
|
2.7
|
25.1
|
1.0
|
OD1
|
D:ASP125
|
2.7
|
27.1
|
1.0
|
O
|
D:HOH941
|
2.7
|
39.2
|
1.0
|
OG
|
D:SER89
|
2.8
|
36.1
|
1.0
|
O
|
D:THR126
|
2.8
|
28.7
|
1.0
|
O
|
D:HOH785
|
2.8
|
38.6
|
1.0
|
CG
|
D:ASP125
|
3.6
|
25.7
|
1.0
|
C
|
D:THR126
|
3.7
|
29.5
|
1.0
|
CG
|
D:ASN87
|
3.7
|
24.2
|
1.0
|
OG
|
D:SER255
|
3.8
|
27.9
|
1.0
|
O
|
D:ASP125
|
3.8
|
25.8
|
1.0
|
CB
|
D:SER89
|
3.9
|
32.1
|
1.0
|
NZ
|
D:LYS282
|
4.0
|
26.8
|
1.0
|
C
|
D:ASP125
|
4.1
|
25.3
|
1.0
|
N
|
D:SER89
|
4.2
|
28.7
|
1.0
|
NH2
|
D:ARG85
|
4.2
|
25.9
|
1.0
|
CA
|
D:LYS127
|
4.2
|
34.4
|
1.0
|
ND2
|
D:ASN87
|
4.3
|
25.1
|
1.0
|
CB
|
D:ASP125
|
4.3
|
22.5
|
1.0
|
N
|
D:LYS127
|
4.3
|
31.5
|
1.0
|
OD2
|
D:ASP125
|
4.4
|
26.6
|
1.0
|
N
|
D:THR126
|
4.5
|
26.1
|
1.0
|
O
|
D:HOH937
|
4.5
|
42.9
|
1.0
|
O
|
D:HOH807
|
4.6
|
29.9
|
1.0
|
CA
|
D:SER89
|
4.6
|
30.5
|
1.0
|
O
|
D:LYS127
|
4.6
|
36.9
|
1.0
|
CA
|
D:THR126
|
4.7
|
27.6
|
1.0
|
N
|
D:PHE88
|
4.7
|
24.5
|
1.0
|
C
|
D:LYS127
|
4.7
|
36.6
|
1.0
|
CA
|
D:ASP125
|
4.9
|
23.1
|
1.0
|
CB
|
D:ASN87
|
4.9
|
21.7
|
1.0
|
CA
|
D:ASN87
|
5.0
|
21.4
|
1.0
|
CB
|
D:SER255
|
5.0
|
26.6
|
1.0
|
|
Potassium binding site 5 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 5 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K604
b:78.9
occ:1.00
|
O
|
E:HOH860
|
2.6
|
45.4
|
1.0
|
OD1
|
E:ASP125
|
2.7
|
48.0
|
1.0
|
OD1
|
E:ASN87
|
2.8
|
45.9
|
1.0
|
OG
|
E:SER89
|
2.8
|
57.1
|
1.0
|
O
|
E:THR126
|
2.8
|
49.7
|
1.0
|
OG
|
E:SER255
|
3.6
|
42.5
|
1.0
|
CG
|
E:ASP125
|
3.7
|
48.4
|
1.0
|
C
|
E:THR126
|
3.7
|
49.8
|
1.0
|
CG
|
E:ASN87
|
3.8
|
45.3
|
1.0
|
NZ
|
E:LYS282
|
3.9
|
45.6
|
1.0
|
CB
|
E:SER89
|
3.9
|
54.4
|
1.0
|
O
|
E:ASP125
|
4.0
|
45.0
|
1.0
|
NH2
|
E:ARG85
|
4.2
|
40.0
|
1.0
|
CA
|
E:LYS127
|
4.3
|
53.1
|
1.0
|
C
|
E:ASP125
|
4.3
|
45.4
|
1.0
|
N
|
E:SER89
|
4.3
|
51.9
|
1.0
|
N
|
E:LYS127
|
4.3
|
51.2
|
1.0
|
ND2
|
E:ASN87
|
4.4
|
45.5
|
1.0
|
CB
|
E:ASP125
|
4.4
|
45.6
|
1.0
|
OD2
|
E:ASP125
|
4.4
|
50.7
|
1.0
|
O
|
E:LYS127
|
4.5
|
54.8
|
1.0
|
N
|
E:THR126
|
4.6
|
46.3
|
1.0
|
CA
|
E:SER89
|
4.6
|
53.2
|
1.0
|
C
|
E:LYS127
|
4.7
|
54.8
|
1.0
|
CA
|
E:THR126
|
4.7
|
47.8
|
1.0
|
CB
|
E:SER255
|
4.8
|
42.0
|
1.0
|
N
|
E:PHE88
|
4.9
|
47.8
|
1.0
|
CA
|
E:ASP125
|
5.0
|
44.6
|
1.0
|
|
Potassium binding site 6 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 6 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K604
b:66.7
occ:1.00
|
OD1
|
F:ASP125
|
2.6
|
41.0
|
1.0
|
OD1
|
F:ASN87
|
2.7
|
40.6
|
1.0
|
O
|
F:THR126
|
2.7
|
41.3
|
1.0
|
O
|
F:HOH754
|
2.8
|
42.4
|
1.0
|
OG
|
F:SER89
|
2.9
|
49.6
|
1.0
|
O
|
F:HOH973
|
3.1
|
54.6
|
1.0
|
CG
|
F:ASP125
|
3.5
|
40.6
|
1.0
|
C
|
F:THR126
|
3.6
|
41.6
|
1.0
|
O
|
F:ASP125
|
3.7
|
35.3
|
1.0
|
OG
|
F:SER255
|
3.7
|
34.6
|
1.0
|
CG
|
F:ASN87
|
3.8
|
39.3
|
1.0
|
NZ
|
F:LYS282
|
3.9
|
32.6
|
1.0
|
CB
|
F:SER89
|
4.0
|
47.7
|
1.0
|
C
|
F:ASP125
|
4.0
|
35.6
|
1.0
|
CB
|
F:ASP125
|
4.2
|
35.5
|
1.0
|
NH2
|
F:ARG85
|
4.2
|
36.4
|
1.0
|
N
|
F:SER89
|
4.2
|
46.0
|
1.0
|
N
|
F:LYS127
|
4.3
|
43.6
|
1.0
|
CA
|
F:LYS127
|
4.3
|
46.3
|
1.0
|
OD2
|
F:ASP125
|
4.3
|
42.6
|
1.0
|
ND2
|
F:ASN87
|
4.4
|
39.7
|
1.0
|
N
|
F:THR126
|
4.4
|
37.1
|
1.0
|
O
|
F:HOH876
|
4.4
|
53.0
|
1.0
|
CA
|
F:THR126
|
4.6
|
39.3
|
1.0
|
CA
|
F:SER89
|
4.6
|
47.3
|
1.0
|
O
|
F:HOH745
|
4.7
|
32.3
|
1.0
|
O
|
F:LYS127
|
4.7
|
48.8
|
1.0
|
N
|
F:PHE88
|
4.7
|
40.9
|
1.0
|
CA
|
F:ASP125
|
4.7
|
34.5
|
1.0
|
C
|
F:LYS127
|
4.8
|
48.2
|
1.0
|
CB
|
F:ASN87
|
4.9
|
37.2
|
1.0
|
CA
|
F:ASN87
|
4.9
|
37.0
|
1.0
|
CB
|
F:SER255
|
4.9
|
33.3
|
1.0
|
|
Potassium binding site 7 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 7 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K605
b:45.7
occ:1.00
|
OD1
|
G:ASP125
|
2.6
|
28.8
|
1.0
|
O
|
G:HOH927
|
2.7
|
35.1
|
1.0
|
OD1
|
G:ASN87
|
2.7
|
28.3
|
1.0
|
O
|
G:THR126
|
2.8
|
26.7
|
1.0
|
O
|
G:HOH847
|
2.8
|
45.6
|
1.0
|
OG
|
G:SER89
|
2.9
|
39.1
|
1.0
|
CG
|
G:ASP125
|
3.5
|
28.7
|
1.0
|
OG
|
G:SER255
|
3.7
|
28.5
|
1.0
|
C
|
G:THR126
|
3.7
|
27.6
|
1.0
|
CG
|
G:ASN87
|
3.7
|
28.4
|
1.0
|
NZ
|
G:LYS282
|
3.9
|
27.0
|
1.0
|
O
|
G:ASP125
|
3.9
|
26.6
|
1.0
|
CB
|
G:SER89
|
4.0
|
34.4
|
1.0
|
NH2
|
G:ARG85
|
4.1
|
29.9
|
1.0
|
C
|
G:ASP125
|
4.2
|
26.2
|
1.0
|
CB
|
G:ASP125
|
4.3
|
24.2
|
1.0
|
OD2
|
G:ASP125
|
4.3
|
30.9
|
1.0
|
ND2
|
G:ASN87
|
4.3
|
28.5
|
1.0
|
N
|
G:SER89
|
4.3
|
29.6
|
1.0
|
CA
|
G:LYS127
|
4.4
|
31.2
|
1.0
|
N
|
G:LYS127
|
4.4
|
29.3
|
1.0
|
O
|
G:HOH931
|
4.4
|
42.0
|
1.0
|
O
|
G:HOH924
|
4.4
|
64.8
|
1.0
|
N
|
G:THR126
|
4.6
|
25.8
|
1.0
|
O
|
G:HOH760
|
4.6
|
27.9
|
1.0
|
O
|
G:LYS127
|
4.7
|
34.5
|
1.0
|
CA
|
G:SER89
|
4.7
|
32.2
|
1.0
|
CA
|
G:THR126
|
4.7
|
25.9
|
1.0
|
C
|
G:LYS127
|
4.8
|
33.3
|
1.0
|
N
|
G:PHE88
|
4.8
|
26.0
|
1.0
|
CA
|
G:ASP125
|
4.9
|
24.2
|
1.0
|
CB
|
G:ASN87
|
4.9
|
25.5
|
1.0
|
CB
|
G:SER255
|
4.9
|
26.6
|
1.0
|
O2
|
G:OXL603
|
5.0
|
32.3
|
1.0
|
CA
|
G:ASN87
|
5.0
|
25.0
|
1.0
|
|
Potassium binding site 8 out
of 8 in 7fsc
Go back to
Potassium Binding Sites List in 7fsc
Potassium binding site 8 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 42
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 42 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K604
b:45.4
occ:1.00
|
O
|
H:HOH994
|
2.3
|
47.8
|
1.0
|
OD1
|
H:ASP125
|
2.6
|
27.6
|
1.0
|
OD1
|
H:ASN87
|
2.7
|
28.9
|
1.0
|
O
|
H:HOH923
|
2.7
|
43.2
|
1.0
|
O
|
H:THR126
|
2.8
|
26.6
|
1.0
|
OG
|
H:SER89
|
2.9
|
36.0
|
1.0
|
CG
|
H:ASP125
|
3.5
|
26.8
|
1.0
|
OG
|
H:SER255
|
3.7
|
25.1
|
1.0
|
C
|
H:THR126
|
3.7
|
28.1
|
1.0
|
CG
|
H:ASN87
|
3.7
|
27.1
|
1.0
|
NZ
|
H:LYS282
|
3.8
|
25.4
|
1.0
|
O
|
H:ASP125
|
3.8
|
25.4
|
1.0
|
CB
|
H:SER89
|
4.0
|
33.2
|
1.0
|
C
|
H:ASP125
|
4.1
|
24.9
|
1.0
|
NH2
|
H:ARG85
|
4.2
|
27.2
|
1.0
|
CB
|
H:ASP125
|
4.2
|
23.6
|
1.0
|
OD2
|
H:ASP125
|
4.3
|
28.5
|
1.0
|
ND2
|
H:ASN87
|
4.3
|
26.9
|
1.0
|
N
|
H:SER89
|
4.3
|
29.9
|
1.0
|
O
|
H:HOH902
|
4.3
|
47.7
|
1.0
|
N
|
H:LYS127
|
4.4
|
30.2
|
1.0
|
CA
|
H:LYS127
|
4.4
|
33.3
|
1.0
|
O
|
H:HOH782
|
4.4
|
24.5
|
1.0
|
N
|
H:THR126
|
4.5
|
25.8
|
1.0
|
CA
|
H:THR126
|
4.7
|
27.1
|
1.0
|
CA
|
H:SER89
|
4.7
|
32.2
|
1.0
|
O
|
H:LYS127
|
4.7
|
35.2
|
1.0
|
N
|
H:PHE88
|
4.8
|
24.2
|
1.0
|
CA
|
H:ASP125
|
4.8
|
23.3
|
1.0
|
C
|
H:LYS127
|
4.8
|
35.3
|
1.0
|
CB
|
H:SER255
|
4.9
|
25.2
|
1.0
|
CB
|
H:ASN87
|
4.9
|
23.6
|
1.0
|
O3
|
H:OXL602
|
4.9
|
29.6
|
1.0
|
CA
|
H:ASN87
|
5.0
|
22.8
|
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 19:04:11 2024
|