Potassium in PDB 7fs0: Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
Enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
All present enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8:
2.7.1.40;
Protein crystallography data
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8, PDB code: 7fs0
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)
|
189.45 /
2.41
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
209.002,
113.344,
189.484,
90,
91.12,
90
|
R / Rfree (%)
|
21.9 /
25.3
|
Other elements in 7fs0:
The structure of Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8 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 8
(pdb code 7fs0). 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 8, PDB code: 7fs0:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 1 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K604
b:149.1
occ:1.00
|
O
|
A:THR126
|
2.5
|
100.9
|
1.0
|
OD1
|
A:ASP125
|
2.6
|
97.1
|
1.0
|
OD1
|
A:ASN87
|
3.1
|
100.7
|
1.0
|
OG
|
A:SER89
|
3.1
|
108.0
|
1.0
|
OG
|
A:SER255
|
3.3
|
96.9
|
1.0
|
C
|
A:THR126
|
3.5
|
100.5
|
1.0
|
CG
|
A:ASP125
|
3.6
|
96.3
|
1.0
|
NZ
|
A:LYS282
|
3.8
|
87.2
|
1.0
|
CA
|
A:LYS127
|
4.0
|
104.1
|
1.0
|
O
|
A:ASP125
|
4.0
|
93.2
|
1.0
|
N
|
A:LYS127
|
4.1
|
102.2
|
1.0
|
CB
|
A:SER89
|
4.2
|
105.4
|
1.0
|
CG
|
A:ASN87
|
4.2
|
99.9
|
1.0
|
C
|
A:ASP125
|
4.2
|
93.2
|
1.0
|
O
|
A:LYS127
|
4.3
|
105.2
|
1.0
|
C
|
A:LYS127
|
4.4
|
105.4
|
1.0
|
CB
|
A:ASP125
|
4.4
|
92.4
|
1.0
|
OD2
|
A:ASP125
|
4.4
|
98.1
|
1.0
|
N
|
A:THR126
|
4.5
|
95.2
|
1.0
|
CB
|
A:SER255
|
4.5
|
94.0
|
1.0
|
N
|
A:SER89
|
4.5
|
102.5
|
1.0
|
NH2
|
A:ARG85
|
4.5
|
100.0
|
1.0
|
CA
|
A:THR126
|
4.6
|
97.8
|
1.0
|
ND2
|
A:ASN87
|
4.8
|
100.7
|
1.0
|
CA
|
A:SER89
|
4.8
|
104.1
|
1.0
|
CA
|
A:ASP125
|
4.9
|
91.0
|
1.0
|
N
|
A:PHE88
|
4.9
|
98.5
|
1.0
|
O2
|
A:OXL602
|
5.0
|
144.2
|
1.0
|
|
Potassium binding site 2 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 2 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K604
b:130.3
occ:1.00
|
OG
|
B:SER89
|
2.6
|
99.1
|
1.0
|
OD1
|
B:ASN87
|
2.8
|
91.4
|
1.0
|
O
|
B:THR126
|
3.0
|
92.5
|
1.0
|
OD1
|
B:ASP125
|
3.2
|
90.0
|
1.0
|
CB
|
B:SER89
|
3.6
|
96.8
|
1.0
|
OG
|
B:SER255
|
3.8
|
77.5
|
1.0
|
CG
|
B:ASN87
|
3.9
|
90.8
|
1.0
|
C
|
B:THR126
|
4.0
|
92.0
|
1.0
|
CG
|
B:ASP125
|
4.1
|
89.4
|
1.0
|
NZ
|
B:LYS282
|
4.1
|
82.7
|
1.0
|
CA
|
B:LYS127
|
4.1
|
96.0
|
1.0
|
N
|
B:SER89
|
4.3
|
94.0
|
1.0
|
O
|
B:LYS127
|
4.3
|
98.4
|
1.0
|
ND2
|
B:ASN87
|
4.4
|
91.5
|
1.0
|
O
|
B:ASP125
|
4.5
|
84.8
|
1.0
|
N
|
B:LYS127
|
4.5
|
93.8
|
1.0
|
CA
|
B:SER89
|
4.5
|
95.5
|
1.0
|
NH2
|
B:ARG85
|
4.5
|
79.8
|
1.0
|
C
|
B:LYS127
|
4.5
|
98.2
|
1.0
|
C
|
B:ASP125
|
4.8
|
85.0
|
1.0
|
OD2
|
B:ASP125
|
4.8
|
91.0
|
1.0
|
CB
|
B:ASP125
|
4.8
|
84.8
|
1.0
|
CB
|
B:SER255
|
5.0
|
75.6
|
1.0
|
O4
|
B:OXL602
|
5.0
|
80.0
|
1.0
|
|
Potassium binding site 3 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 3 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K604
b:100.5
occ:1.00
|
OD1
|
C:ASN87
|
2.6
|
65.5
|
1.0
|
OD1
|
C:ASP125
|
2.8
|
67.1
|
1.0
|
O
|
C:THR126
|
3.0
|
59.2
|
1.0
|
OG
|
C:SER89
|
3.0
|
64.7
|
1.0
|
CG
|
C:ASP125
|
3.6
|
65.1
|
1.0
|
CG
|
C:ASN87
|
3.7
|
64.0
|
1.0
|
OG
|
C:SER255
|
3.8
|
47.1
|
1.0
|
CB
|
C:SER89
|
3.9
|
62.2
|
1.0
|
C
|
C:THR126
|
3.9
|
59.2
|
1.0
|
NZ
|
C:LYS282
|
4.0
|
61.0
|
1.0
|
O
|
C:ASP125
|
4.1
|
54.6
|
1.0
|
NH2
|
C:ARG85
|
4.1
|
70.8
|
1.0
|
ND2
|
C:ASN87
|
4.2
|
64.7
|
1.0
|
N
|
C:SER89
|
4.3
|
59.4
|
1.0
|
O
|
C:HOH719
|
4.3
|
55.9
|
1.0
|
CB
|
C:ASP125
|
4.3
|
56.9
|
1.0
|
OD2
|
C:ASP125
|
4.4
|
69.2
|
1.0
|
CA
|
C:LYS127
|
4.4
|
63.1
|
1.0
|
C
|
C:ASP125
|
4.4
|
55.1
|
1.0
|
N
|
C:LYS127
|
4.5
|
61.1
|
1.0
|
O
|
C:LYS127
|
4.7
|
65.8
|
1.0
|
CA
|
C:SER89
|
4.7
|
61.1
|
1.0
|
N
|
C:PHE88
|
4.8
|
58.0
|
1.0
|
C
|
C:LYS127
|
4.8
|
64.9
|
1.0
|
N
|
C:THR126
|
4.8
|
55.5
|
1.0
|
CB
|
C:ASN87
|
4.9
|
60.6
|
1.0
|
O4
|
C:OXL602
|
4.9
|
78.9
|
1.0
|
CA
|
C:ASN87
|
5.0
|
59.0
|
1.0
|
CB
|
C:SER255
|
5.0
|
46.0
|
1.0
|
CA
|
C:THR126
|
5.0
|
56.3
|
1.0
|
|
Potassium binding site 4 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 4 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K604
b:70.1
occ:1.00
|
OD1
|
D:ASP125
|
2.7
|
49.1
|
1.0
|
O
|
D:THR126
|
2.7
|
49.2
|
1.0
|
OD1
|
D:ASN87
|
2.8
|
38.9
|
1.0
|
OG
|
D:SER89
|
2.9
|
48.8
|
1.0
|
CG
|
D:ASP125
|
3.6
|
46.1
|
1.0
|
OG
|
D:SER255
|
3.6
|
44.6
|
1.0
|
C
|
D:THR126
|
3.7
|
49.5
|
1.0
|
CG
|
D:ASN87
|
3.9
|
38.0
|
1.0
|
NZ
|
D:LYS282
|
3.9
|
44.9
|
1.0
|
CB
|
D:SER89
|
3.9
|
46.7
|
1.0
|
O
|
D:ASP125
|
4.0
|
43.0
|
1.0
|
CA
|
D:LYS127
|
4.2
|
55.7
|
1.0
|
C
|
D:ASP125
|
4.3
|
43.0
|
1.0
|
N
|
D:SER89
|
4.3
|
43.9
|
1.0
|
N
|
D:LYS127
|
4.3
|
52.5
|
1.0
|
CB
|
D:ASP125
|
4.3
|
42.2
|
1.0
|
NH2
|
D:ARG85
|
4.3
|
42.4
|
1.0
|
OD2
|
D:ASP125
|
4.4
|
45.8
|
1.0
|
ND2
|
D:ASN87
|
4.4
|
38.7
|
1.0
|
O
|
D:LYS127
|
4.5
|
60.9
|
1.0
|
C
|
D:LYS127
|
4.6
|
59.7
|
1.0
|
N
|
D:THR126
|
4.6
|
44.0
|
1.0
|
CA
|
D:SER89
|
4.7
|
45.9
|
1.0
|
O
|
D:HOH847
|
4.7
|
54.9
|
1.0
|
CA
|
D:THR126
|
4.8
|
45.7
|
1.0
|
N
|
D:PHE88
|
4.8
|
38.6
|
1.0
|
CB
|
D:SER255
|
4.8
|
44.4
|
1.0
|
CA
|
D:ASP125
|
4.9
|
41.2
|
1.0
|
|
Potassium binding site 5 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 5 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K604
b:127.6
occ:1.00
|
O
|
E:THR126
|
2.7
|
85.7
|
1.0
|
OD1
|
E:ASP125
|
2.8
|
85.2
|
1.0
|
OG
|
E:SER89
|
2.9
|
92.8
|
1.0
|
OD1
|
E:ASN87
|
3.0
|
77.4
|
1.0
|
OG
|
E:SER255
|
3.4
|
74.2
|
1.0
|
C
|
E:THR126
|
3.7
|
85.5
|
1.0
|
CG
|
E:ASP125
|
3.8
|
84.2
|
1.0
|
NZ
|
E:LYS282
|
3.9
|
71.7
|
1.0
|
CB
|
E:SER89
|
4.0
|
90.3
|
1.0
|
CA
|
E:LYS127
|
4.0
|
89.9
|
1.0
|
CG
|
E:ASN87
|
4.1
|
77.0
|
1.0
|
O
|
E:ASP125
|
4.2
|
80.1
|
1.0
|
O
|
E:LYS127
|
4.2
|
91.9
|
1.0
|
N
|
E:LYS127
|
4.3
|
87.6
|
1.0
|
C
|
E:LYS127
|
4.4
|
91.8
|
1.0
|
N
|
E:SER89
|
4.5
|
86.4
|
1.0
|
C
|
E:ASP125
|
4.5
|
80.2
|
1.0
|
NH2
|
E:ARG85
|
4.6
|
67.6
|
1.0
|
CB
|
E:SER255
|
4.6
|
72.8
|
1.0
|
OD2
|
E:ASP125
|
4.6
|
85.6
|
1.0
|
CB
|
E:ASP125
|
4.6
|
80.5
|
1.0
|
ND2
|
E:ASN87
|
4.7
|
76.9
|
1.0
|
CA
|
E:SER89
|
4.7
|
88.9
|
1.0
|
N
|
E:THR126
|
4.8
|
81.2
|
1.0
|
CA
|
E:THR126
|
4.8
|
82.9
|
1.0
|
O3
|
E:OXL602
|
4.9
|
89.8
|
1.0
|
|
Potassium binding site 6 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 6 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K604
b:118.5
occ:1.00
|
O
|
F:THR126
|
2.7
|
70.2
|
1.0
|
OD1
|
F:ASP125
|
2.8
|
71.3
|
1.0
|
OD1
|
F:ASN87
|
2.9
|
60.6
|
1.0
|
OG
|
F:SER89
|
2.9
|
71.9
|
1.0
|
OG
|
F:SER255
|
3.6
|
54.2
|
1.0
|
C
|
F:THR126
|
3.7
|
70.2
|
1.0
|
CG
|
F:ASP125
|
3.7
|
68.5
|
1.0
|
NZ
|
F:LYS282
|
3.9
|
51.7
|
1.0
|
CB
|
F:SER89
|
4.0
|
70.5
|
1.0
|
CG
|
F:ASN87
|
4.0
|
61.0
|
1.0
|
CA
|
F:LYS127
|
4.1
|
76.1
|
1.0
|
O
|
F:ASP125
|
4.1
|
61.3
|
1.0
|
N
|
F:LYS127
|
4.2
|
73.1
|
1.0
|
C
|
F:ASP125
|
4.3
|
62.1
|
1.0
|
N
|
F:SER89
|
4.4
|
68.9
|
1.0
|
O
|
F:LYS127
|
4.4
|
79.5
|
1.0
|
NH2
|
F:ARG85
|
4.5
|
63.5
|
1.0
|
CB
|
F:ASP125
|
4.5
|
62.7
|
1.0
|
C
|
F:LYS127
|
4.5
|
78.8
|
1.0
|
OD2
|
F:ASP125
|
4.5
|
69.3
|
1.0
|
ND2
|
F:ASN87
|
4.6
|
62.3
|
1.0
|
N
|
F:THR126
|
4.7
|
64.3
|
1.0
|
CA
|
F:SER89
|
4.7
|
70.1
|
1.0
|
CB
|
F:SER255
|
4.8
|
52.9
|
1.0
|
CA
|
F:THR126
|
4.8
|
66.9
|
1.0
|
N
|
F:PHE88
|
4.9
|
63.8
|
1.0
|
|
Potassium binding site 7 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 7 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K604
b:89.0
occ:1.00
|
OD1
|
G:ASP125
|
2.8
|
53.0
|
1.0
|
O
|
G:THR126
|
2.9
|
48.2
|
1.0
|
OD1
|
G:ASN87
|
2.9
|
49.5
|
1.0
|
OG
|
G:SER89
|
3.0
|
55.5
|
1.0
|
O
|
G:HOH759
|
3.5
|
63.7
|
1.0
|
OG
|
G:SER255
|
3.6
|
43.7
|
1.0
|
CG
|
G:ASP125
|
3.7
|
50.6
|
1.0
|
NZ
|
G:LYS282
|
3.8
|
40.5
|
1.0
|
C
|
G:THR126
|
3.9
|
47.6
|
1.0
|
CG
|
G:ASN87
|
4.0
|
47.9
|
1.0
|
CB
|
G:SER89
|
4.0
|
53.2
|
1.0
|
NH2
|
G:ARG85
|
4.3
|
62.3
|
1.0
|
CA
|
G:LYS127
|
4.3
|
50.7
|
1.0
|
O
|
G:ASP125
|
4.4
|
46.4
|
1.0
|
OD2
|
G:ASP125
|
4.4
|
51.8
|
1.0
|
ND2
|
G:ASN87
|
4.4
|
49.2
|
1.0
|
O
|
G:LYS127
|
4.5
|
53.0
|
1.0
|
N
|
G:LYS127
|
4.5
|
48.4
|
1.0
|
N
|
G:SER89
|
4.6
|
49.2
|
1.0
|
CB
|
G:ASP125
|
4.6
|
44.8
|
1.0
|
C
|
G:ASP125
|
4.6
|
44.9
|
1.0
|
O2
|
G:OXL602
|
4.7
|
58.2
|
1.0
|
C
|
G:LYS127
|
4.7
|
52.4
|
1.0
|
CB
|
G:SER255
|
4.8
|
43.0
|
1.0
|
CA
|
G:SER89
|
4.8
|
52.1
|
1.0
|
N
|
G:THR126
|
4.9
|
44.6
|
1.0
|
|
Potassium binding site 8 out
of 8 in 7fs0
Go back to
Potassium Binding Sites List in 7fs0
Potassium binding site 8 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Allosteric Modulator 8
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 8 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K604
b:76.6
occ:1.00
|
OD1
|
H:ASP125
|
2.7
|
44.1
|
1.0
|
O
|
H:THR126
|
2.7
|
45.5
|
1.0
|
OD1
|
H:ASN87
|
2.8
|
43.5
|
1.0
|
OG
|
H:SER89
|
2.9
|
54.3
|
1.0
|
OG
|
H:SER255
|
3.6
|
37.5
|
1.0
|
CG
|
H:ASP125
|
3.7
|
41.6
|
1.0
|
C
|
H:THR126
|
3.7
|
45.7
|
1.0
|
NZ
|
H:LYS282
|
3.9
|
42.1
|
1.0
|
CG
|
H:ASN87
|
3.9
|
39.5
|
1.0
|
CB
|
H:SER89
|
3.9
|
50.9
|
1.0
|
O
|
H:ASP125
|
4.0
|
38.8
|
1.0
|
CA
|
H:LYS127
|
4.1
|
52.8
|
1.0
|
O
|
H:HOH793
|
4.2
|
52.5
|
1.0
|
N
|
H:LYS127
|
4.3
|
49.1
|
1.0
|
N
|
H:SER89
|
4.3
|
46.7
|
1.0
|
C
|
H:ASP125
|
4.3
|
38.9
|
1.0
|
NH2
|
H:ARG85
|
4.4
|
39.8
|
1.0
|
CB
|
H:ASP125
|
4.4
|
36.3
|
1.0
|
OD2
|
H:ASP125
|
4.4
|
42.7
|
1.0
|
ND2
|
H:ASN87
|
4.4
|
38.2
|
1.0
|
O
|
H:LYS127
|
4.5
|
56.8
|
1.0
|
C
|
H:LYS127
|
4.6
|
56.6
|
1.0
|
N
|
H:THR126
|
4.7
|
40.2
|
1.0
|
CA
|
H:SER89
|
4.7
|
49.1
|
1.0
|
CA
|
H:THR126
|
4.8
|
41.9
|
1.0
|
CB
|
H:SER255
|
4.8
|
37.1
|
1.0
|
N
|
H:PHE88
|
4.8
|
39.0
|
1.0
|
O3
|
H:OXL602
|
4.9
|
56.5
|
1.0
|
O
|
H:HOH901
|
4.9
|
55.5
|
1.0
|
CA
|
H:ASP125
|
5.0
|
36.5
|
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 18:57:20 2024
|