Potassium in PDB 5sch: Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
Enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
All present enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100:
2.7.1.40;
Protein crystallography data
The structure of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100, PDB code: 5sch
was solved by
A.Lulla,
A.Foller,
A.Nain-Perez,
M.Grotli,
P.Brear,
M.Hyvonen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.73 /
2.09
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
209.023,
113.386,
189.604,
90,
91.33,
90
|
R / Rfree (%)
|
21.3 /
24.6
|
Other elements in 5sch:
The structure of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100 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 Anthraquinone Derivative 100
(pdb code 5sch). 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 Anthraquinone Derivative 100, PDB code: 5sch:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 1 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K604
b:108.3
occ:1.00
|
OD1
|
A:ASN87
|
2.5
|
79.7
|
1.0
|
O
|
A:THR126
|
2.7
|
80.8
|
1.0
|
OD1
|
A:ASP125
|
2.7
|
76.0
|
1.0
|
OG
|
A:SER89
|
2.7
|
84.7
|
1.0
|
C
|
A:THR126
|
3.5
|
80.6
|
1.0
|
CG
|
A:ASP125
|
3.6
|
75.4
|
1.0
|
CG
|
A:ASN87
|
3.6
|
78.6
|
1.0
|
CB
|
A:SER89
|
3.7
|
82.5
|
1.0
|
OG
|
A:SER255
|
3.8
|
72.1
|
1.0
|
O
|
A:ASP125
|
3.9
|
72.5
|
1.0
|
NZ
|
A:LYS282
|
3.9
|
68.6
|
1.0
|
CA
|
A:LYS127
|
4.1
|
85.4
|
1.0
|
N
|
A:SER89
|
4.1
|
80.4
|
1.0
|
C
|
A:ASP125
|
4.1
|
72.5
|
1.0
|
ND2
|
A:ASN87
|
4.2
|
78.8
|
1.0
|
N
|
A:LYS127
|
4.2
|
83.0
|
1.0
|
CB
|
A:ASP125
|
4.3
|
71.2
|
1.0
|
O
|
A:LYS127
|
4.4
|
87.2
|
1.0
|
OD2
|
A:ASP125
|
4.4
|
77.3
|
1.0
|
N
|
A:THR126
|
4.5
|
74.7
|
1.0
|
CA
|
A:SER89
|
4.5
|
81.7
|
1.0
|
NH2
|
A:ARG85
|
4.5
|
63.0
|
1.0
|
C
|
A:LYS127
|
4.6
|
86.9
|
1.0
|
CA
|
A:THR126
|
4.6
|
77.4
|
1.0
|
N
|
A:PHE88
|
4.7
|
76.7
|
1.0
|
CA
|
A:ASP125
|
4.8
|
69.9
|
1.0
|
CB
|
A:ASN87
|
4.8
|
75.6
|
1.0
|
CB
|
A:SER255
|
4.9
|
69.4
|
1.0
|
CA
|
A:ASN87
|
4.9
|
74.5
|
1.0
|
C
|
A:PHE88
|
5.0
|
79.6
|
1.0
|
|
Potassium binding site 2 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 2 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K604
b:89.2
occ:1.00
|
OG
|
B:SER89
|
2.6
|
93.8
|
1.0
|
OD1
|
B:ASN87
|
2.6
|
82.0
|
1.0
|
O
|
B:THR126
|
2.9
|
87.1
|
1.0
|
OD1
|
B:ASP125
|
2.9
|
81.6
|
1.0
|
CB
|
B:SER89
|
3.6
|
91.0
|
1.0
|
OG
|
B:SER255
|
3.7
|
65.9
|
1.0
|
CG
|
B:ASN87
|
3.7
|
81.6
|
1.0
|
C
|
B:THR126
|
3.8
|
86.3
|
1.0
|
CG
|
B:ASP125
|
3.8
|
81.4
|
1.0
|
NZ
|
B:LYS282
|
4.0
|
62.2
|
1.0
|
ND2
|
B:ASN87
|
4.1
|
82.8
|
1.0
|
CA
|
B:LYS127
|
4.2
|
90.6
|
1.0
|
O
|
B:ASP125
|
4.2
|
78.7
|
1.0
|
N
|
B:SER89
|
4.2
|
87.3
|
1.0
|
N
|
B:LYS127
|
4.3
|
88.4
|
1.0
|
O
|
B:LYS127
|
4.4
|
93.0
|
1.0
|
O
|
B:HOH792
|
4.4
|
60.9
|
1.0
|
CA
|
B:SER89
|
4.5
|
89.4
|
1.0
|
C
|
B:ASP125
|
4.5
|
78.8
|
1.0
|
NH2
|
B:ARG85
|
4.5
|
64.6
|
1.0
|
CB
|
B:ASP125
|
4.5
|
78.5
|
1.0
|
C
|
B:LYS127
|
4.6
|
92.6
|
1.0
|
OD2
|
B:ASP125
|
4.6
|
82.7
|
1.0
|
N
|
B:THR126
|
4.8
|
80.4
|
1.0
|
CA
|
B:THR126
|
4.9
|
83.0
|
1.0
|
CB
|
B:SER255
|
4.9
|
64.8
|
1.0
|
N
|
B:PHE88
|
5.0
|
82.2
|
1.0
|
CB
|
B:ASN87
|
5.0
|
79.4
|
1.0
|
|
Potassium binding site 3 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 3 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K605
b:78.2
occ:1.00
|
OD1
|
C:ASN87
|
2.5
|
45.0
|
1.0
|
OD1
|
C:ASP125
|
2.6
|
48.7
|
1.0
|
O
|
C:THR126
|
2.8
|
42.2
|
1.0
|
OG
|
C:SER89
|
2.9
|
50.3
|
1.0
|
CG
|
C:ASP125
|
3.5
|
47.8
|
1.0
|
CG
|
C:ASN87
|
3.5
|
45.7
|
1.0
|
OG
|
C:SER255
|
3.6
|
41.3
|
1.0
|
C
|
C:THR126
|
3.7
|
43.3
|
1.0
|
CB
|
C:SER89
|
3.8
|
48.9
|
1.0
|
NZ
|
C:LYS282
|
3.9
|
40.3
|
1.0
|
O
|
C:ASP125
|
3.9
|
41.9
|
1.0
|
ND2
|
C:ASN87
|
4.0
|
45.0
|
1.0
|
CB
|
C:ASP125
|
4.2
|
42.2
|
1.0
|
C
|
C:ASP125
|
4.2
|
41.7
|
1.0
|
OD2
|
C:ASP125
|
4.3
|
50.4
|
1.0
|
N
|
C:SER89
|
4.3
|
47.7
|
1.0
|
NH2
|
C:ARG85
|
4.3
|
47.9
|
1.0
|
CA
|
C:LYS127
|
4.4
|
47.2
|
1.0
|
N
|
C:LYS127
|
4.4
|
45.5
|
1.0
|
N
|
C:THR126
|
4.5
|
41.3
|
1.0
|
CA
|
C:SER89
|
4.6
|
48.2
|
1.0
|
O
|
C:HOH711
|
4.6
|
43.1
|
1.0
|
O
|
C:LYS127
|
4.6
|
49.9
|
1.0
|
CA
|
C:THR126
|
4.7
|
41.4
|
1.0
|
CB
|
C:ASN87
|
4.8
|
45.4
|
1.0
|
N
|
C:PHE88
|
4.8
|
45.4
|
1.0
|
CA
|
C:ASP125
|
4.8
|
40.9
|
1.0
|
C
|
C:LYS127
|
4.8
|
49.3
|
1.0
|
CB
|
C:SER255
|
4.9
|
38.4
|
1.0
|
O4
|
C:OXL602
|
4.9
|
55.5
|
1.0
|
CA
|
C:ASN87
|
4.9
|
45.6
|
1.0
|
|
Potassium binding site 4 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 4 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K604
b:48.3
occ:1.00
|
OD1
|
D:ASN87
|
2.6
|
35.1
|
1.0
|
OD1
|
D:ASP125
|
2.6
|
36.3
|
1.0
|
O
|
D:THR126
|
2.8
|
37.7
|
1.0
|
O
|
D:HOH904
|
2.8
|
43.8
|
1.0
|
OG
|
D:SER89
|
2.9
|
43.0
|
1.0
|
O
|
D:HOH715
|
3.0
|
37.0
|
1.0
|
CG
|
D:ASP125
|
3.5
|
34.2
|
1.0
|
OG
|
D:SER255
|
3.7
|
35.8
|
1.0
|
C
|
D:THR126
|
3.7
|
38.1
|
1.0
|
CG
|
D:ASN87
|
3.7
|
32.1
|
1.0
|
CB
|
D:SER89
|
3.8
|
38.4
|
1.0
|
O
|
D:ASP125
|
3.9
|
32.8
|
1.0
|
NZ
|
D:LYS282
|
3.9
|
34.2
|
1.0
|
C
|
D:ASP125
|
4.2
|
32.4
|
1.0
|
ND2
|
D:ASN87
|
4.2
|
32.9
|
1.0
|
CB
|
D:ASP125
|
4.2
|
31.4
|
1.0
|
N
|
D:SER89
|
4.3
|
35.5
|
1.0
|
CA
|
D:LYS127
|
4.3
|
43.8
|
1.0
|
N
|
D:LYS127
|
4.3
|
40.9
|
1.0
|
OD2
|
D:ASP125
|
4.3
|
34.5
|
1.0
|
NH2
|
D:ARG85
|
4.3
|
28.4
|
1.0
|
N
|
D:THR126
|
4.5
|
33.4
|
1.0
|
O
|
D:LYS127
|
4.5
|
46.9
|
1.0
|
CA
|
D:SER89
|
4.6
|
37.3
|
1.0
|
O
|
D:HOH911
|
4.7
|
55.7
|
1.0
|
CA
|
D:THR126
|
4.7
|
35.5
|
1.0
|
C
|
D:LYS127
|
4.7
|
46.7
|
1.0
|
N
|
D:PHE88
|
4.8
|
31.5
|
1.0
|
CA
|
D:ASP125
|
4.8
|
31.0
|
1.0
|
CB
|
D:ASN87
|
4.9
|
29.6
|
1.0
|
CB
|
D:SER255
|
4.9
|
33.7
|
1.0
|
CA
|
D:ASN87
|
5.0
|
30.3
|
1.0
|
|
Potassium binding site 5 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 5 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K605
b:134.7
occ:1.00
|
OG
|
E:SER89
|
2.9
|
73.1
|
1.0
|
OD1
|
E:ASN87
|
3.0
|
63.4
|
1.0
|
OD1
|
E:ASP125
|
3.0
|
71.3
|
1.0
|
O
|
E:THR126
|
3.3
|
68.8
|
1.0
|
OG
|
E:SER255
|
3.6
|
57.5
|
1.0
|
NZ
|
E:LYS282
|
3.6
|
45.0
|
1.0
|
CG
|
E:ASP125
|
3.9
|
71.3
|
1.0
|
CG
|
E:ASN87
|
3.9
|
63.4
|
1.0
|
CB
|
E:SER89
|
3.9
|
70.5
|
1.0
|
ND2
|
E:ASN87
|
4.1
|
64.8
|
1.0
|
NH2
|
E:ARG85
|
4.3
|
53.6
|
1.0
|
O3
|
E:OXL602
|
4.3
|
78.8
|
1.0
|
C
|
E:THR126
|
4.3
|
68.9
|
1.0
|
OD2
|
E:ASP125
|
4.5
|
74.7
|
1.0
|
CA
|
E:LYS127
|
4.7
|
72.9
|
1.0
|
CB
|
E:SER255
|
4.7
|
56.4
|
1.0
|
CB
|
E:ASP125
|
4.8
|
66.5
|
1.0
|
O
|
E:ASP125
|
4.8
|
64.8
|
1.0
|
N
|
E:SER89
|
4.8
|
67.4
|
1.0
|
O
|
E:LYS127
|
4.9
|
74.8
|
1.0
|
CA
|
E:SER89
|
4.9
|
68.8
|
1.0
|
N
|
E:LYS127
|
5.0
|
70.7
|
1.0
|
C
|
E:ASP125
|
5.0
|
65.0
|
1.0
|
|
Potassium binding site 6 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 6 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K605
b:87.4
occ:1.00
|
O
|
F:THR126
|
2.7
|
60.7
|
1.0
|
OD1
|
F:ASP125
|
2.7
|
60.3
|
1.0
|
OG
|
F:SER89
|
2.8
|
59.6
|
1.0
|
O
|
F:HOH825
|
2.8
|
54.4
|
1.0
|
OD1
|
F:ASN87
|
2.9
|
51.8
|
1.0
|
OG
|
F:SER255
|
3.4
|
47.9
|
1.0
|
NZ
|
F:LYS282
|
3.6
|
43.8
|
1.0
|
C
|
F:THR126
|
3.7
|
60.2
|
1.0
|
CG
|
F:ASP125
|
3.7
|
58.9
|
1.0
|
CB
|
F:SER89
|
3.8
|
57.9
|
1.0
|
CG
|
F:ASN87
|
3.9
|
51.9
|
1.0
|
O
|
F:ASP125
|
4.2
|
52.0
|
1.0
|
CA
|
F:LYS127
|
4.2
|
64.7
|
1.0
|
N
|
F:LYS127
|
4.3
|
62.5
|
1.0
|
ND2
|
F:ASN87
|
4.3
|
53.9
|
1.0
|
O
|
F:LYS127
|
4.3
|
67.6
|
1.0
|
C
|
F:ASP125
|
4.4
|
52.7
|
1.0
|
OD2
|
F:ASP125
|
4.4
|
61.1
|
1.0
|
CB
|
F:ASP125
|
4.4
|
53.2
|
1.0
|
N
|
F:SER89
|
4.4
|
57.0
|
1.0
|
NH2
|
F:ARG85
|
4.5
|
50.9
|
1.0
|
C
|
F:LYS127
|
4.6
|
66.9
|
1.0
|
N
|
F:THR126
|
4.6
|
54.7
|
1.0
|
CB
|
F:SER255
|
4.6
|
46.4
|
1.0
|
CA
|
F:SER89
|
4.7
|
57.5
|
1.0
|
CA
|
F:THR126
|
4.7
|
57.1
|
1.0
|
O2
|
F:OXL602
|
4.8
|
59.6
|
1.0
|
|
Potassium binding site 7 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 7 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K605
b:73.0
occ:1.00
|
OD1
|
G:ASP125
|
2.7
|
44.9
|
1.0
|
O
|
G:THR126
|
2.8
|
37.8
|
1.0
|
OD1
|
G:ASN87
|
2.8
|
38.6
|
1.0
|
OG
|
G:SER89
|
2.8
|
41.4
|
1.0
|
OG
|
G:SER255
|
3.4
|
34.0
|
1.0
|
CG
|
G:ASP125
|
3.6
|
43.3
|
1.0
|
NZ
|
G:LYS282
|
3.7
|
33.2
|
1.0
|
C
|
G:THR126
|
3.8
|
38.4
|
1.0
|
CG
|
G:ASN87
|
3.8
|
37.7
|
1.0
|
CB
|
G:SER89
|
3.9
|
40.1
|
1.0
|
O
|
G:HOH750
|
4.1
|
39.5
|
1.0
|
ND2
|
G:ASN87
|
4.2
|
36.0
|
1.0
|
O
|
G:ASP125
|
4.3
|
34.1
|
1.0
|
CA
|
G:LYS127
|
4.3
|
41.9
|
1.0
|
OD2
|
G:ASP125
|
4.4
|
45.2
|
1.0
|
O
|
G:LYS127
|
4.4
|
42.8
|
1.0
|
C
|
G:ASP125
|
4.4
|
34.6
|
1.0
|
CB
|
G:ASP125
|
4.4
|
36.6
|
1.0
|
NH2
|
G:ARG85
|
4.4
|
40.7
|
1.0
|
N
|
G:LYS127
|
4.4
|
39.7
|
1.0
|
N
|
G:SER89
|
4.5
|
37.6
|
1.0
|
CB
|
G:SER255
|
4.6
|
33.7
|
1.0
|
O2
|
G:OXL602
|
4.6
|
43.1
|
1.0
|
N
|
G:THR126
|
4.7
|
35.3
|
1.0
|
C
|
G:LYS127
|
4.7
|
42.7
|
1.0
|
CA
|
G:SER89
|
4.7
|
39.5
|
1.0
|
CA
|
G:THR126
|
4.8
|
36.7
|
1.0
|
O
|
G:HOH717
|
5.0
|
33.9
|
1.0
|
|
Potassium binding site 8 out
of 8 in 5sch
Go back to
Potassium Binding Sites List in 5sch
Potassium binding site 8 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 100
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 Anthraquinone Derivative 100 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K604
b:54.0
occ:1.00
|
OD1
|
H:ASN87
|
2.6
|
35.9
|
1.0
|
OD1
|
H:ASP125
|
2.6
|
34.3
|
1.0
|
O
|
H:THR126
|
2.7
|
33.8
|
1.0
|
O
|
H:HOH845
|
2.7
|
42.3
|
1.0
|
OG
|
H:SER89
|
2.8
|
43.5
|
1.0
|
CG
|
H:ASP125
|
3.5
|
34.2
|
1.0
|
C
|
H:THR126
|
3.6
|
33.8
|
1.0
|
OG
|
H:SER255
|
3.6
|
35.0
|
1.0
|
CG
|
H:ASN87
|
3.7
|
32.2
|
1.0
|
CB
|
H:SER89
|
3.8
|
39.6
|
1.0
|
O
|
H:ASP125
|
3.9
|
28.8
|
1.0
|
C
|
H:ASP125
|
4.1
|
28.6
|
1.0
|
ND2
|
H:ASN87
|
4.2
|
31.5
|
1.0
|
NZ
|
H:LYS282
|
4.2
|
30.0
|
1.0
|
N
|
H:SER89
|
4.2
|
36.2
|
1.0
|
CA
|
H:LYS127
|
4.2
|
41.4
|
1.0
|
CB
|
H:ASP125
|
4.2
|
28.3
|
1.0
|
N
|
H:LYS127
|
4.2
|
37.1
|
1.0
|
OD2
|
H:ASP125
|
4.4
|
38.2
|
1.0
|
O
|
H:HOH826
|
4.4
|
57.1
|
1.0
|
NH2
|
H:ARG85
|
4.4
|
33.6
|
1.0
|
N
|
H:THR126
|
4.4
|
29.4
|
1.0
|
O
|
H:LYS127
|
4.5
|
43.6
|
1.0
|
CA
|
H:SER89
|
4.5
|
37.9
|
1.0
|
CA
|
H:THR126
|
4.6
|
30.4
|
1.0
|
C
|
H:LYS127
|
4.7
|
44.0
|
1.0
|
N
|
H:PHE88
|
4.7
|
31.7
|
1.0
|
O
|
H:HOH711
|
4.7
|
28.4
|
1.0
|
O
|
H:HOH924
|
4.7
|
54.3
|
1.0
|
CA
|
H:ASP125
|
4.8
|
27.5
|
1.0
|
CB
|
H:ASN87
|
4.9
|
29.3
|
1.0
|
CB
|
H:SER255
|
4.9
|
33.3
|
1.0
|
CA
|
H:ASN87
|
4.9
|
30.3
|
1.0
|
|
Reference:
A.Nain-Perez,
A.Foller Fuchtbauer,
L.Haversen,
A.Lulla,
C.Gao,
J.Matic,
L.Monjas,
A.Rodriguez,
P.Brear,
W.Kim,
M.Hyvonen,
J.Boren,
A.Mardinoglu,
M.Uhlen,
M.Grotli.
Anthraquinone Derivatives As Adp-Competitive Inhibitors of Liver Pyruvate Kinase. Eur.J.Med.Chem. V. 234 14270 2022.
ISSN: ISSN 0223-5234
PubMed: 35290845
DOI: 10.1016/J.EJMECH.2022.114270
Page generated: Mon Aug 12 14:28:37 2024
|