Potassium in PDB 5sci: Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
Enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
All present enzymatic activity of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105:
2.7.1.40;
Protein crystallography data
The structure of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105, PDB code: 5sci
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)
|
188.28 /
2.16
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
207.651,
112.839,
188.356,
90,
91.67,
90
|
R / Rfree (%)
|
20.6 /
22.9
|
Other elements in 5sci:
The structure of Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105 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 105
(pdb code 5sci). 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 105, PDB code: 5sci:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 1 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K604
b:120.6
occ:1.00
|
OD1
|
A:ASP125
|
2.6
|
75.5
|
1.0
|
OD1
|
A:ASN87
|
2.6
|
78.5
|
1.0
|
O
|
A:THR126
|
2.7
|
80.8
|
1.0
|
OG
|
A:SER89
|
2.7
|
83.7
|
1.0
|
OG
|
A:SER255
|
3.5
|
74.7
|
1.0
|
CG
|
A:ASP125
|
3.5
|
75.6
|
1.0
|
C
|
A:THR126
|
3.6
|
80.5
|
1.0
|
CG
|
A:ASN87
|
3.7
|
78.0
|
1.0
|
CB
|
A:SER89
|
3.7
|
81.0
|
1.0
|
NZ
|
A:LYS282
|
3.9
|
65.0
|
1.0
|
O
|
A:ASP125
|
3.9
|
73.3
|
1.0
|
ND2
|
A:ASN87
|
4.2
|
78.7
|
1.0
|
CA
|
A:LYS127
|
4.2
|
85.0
|
1.0
|
C
|
A:ASP125
|
4.2
|
73.7
|
1.0
|
N
|
A:SER89
|
4.2
|
78.7
|
1.0
|
N
|
A:LYS127
|
4.3
|
82.6
|
1.0
|
CB
|
A:ASP125
|
4.3
|
73.0
|
1.0
|
OD2
|
A:ASP125
|
4.3
|
76.6
|
1.0
|
NH2
|
A:ARG85
|
4.4
|
66.0
|
1.0
|
N
|
A:THR126
|
4.5
|
75.5
|
1.0
|
O
|
A:LYS127
|
4.6
|
87.0
|
1.0
|
CA
|
A:SER89
|
4.6
|
79.6
|
1.0
|
CA
|
A:THR126
|
4.6
|
77.4
|
1.0
|
C
|
A:LYS127
|
4.7
|
86.8
|
1.0
|
CB
|
A:SER255
|
4.8
|
71.5
|
1.0
|
N
|
A:PHE88
|
4.8
|
76.6
|
1.0
|
CA
|
A:ASP125
|
4.9
|
72.0
|
1.0
|
CB
|
A:ASN87
|
4.9
|
75.4
|
1.0
|
|
Potassium binding site 2 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 2 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K604
b:86.3
occ:1.00
|
OG
|
B:SER89
|
2.5
|
71.1
|
1.0
|
OD1
|
B:ASN87
|
2.7
|
61.4
|
1.0
|
O
|
B:THR126
|
2.8
|
69.8
|
1.0
|
OD1
|
B:ASP125
|
2.8
|
70.1
|
1.0
|
OG
|
B:SER255
|
3.5
|
54.0
|
1.0
|
CB
|
B:SER89
|
3.6
|
68.9
|
1.0
|
C
|
B:THR126
|
3.7
|
69.7
|
1.0
|
CG
|
B:ASP125
|
3.8
|
70.0
|
1.0
|
CG
|
B:ASN87
|
3.8
|
61.6
|
1.0
|
NZ
|
B:LYS282
|
3.9
|
60.6
|
1.0
|
CA
|
B:LYS127
|
4.1
|
74.5
|
1.0
|
ND2
|
B:ASN87
|
4.2
|
62.5
|
1.0
|
O
|
B:ASP125
|
4.2
|
61.5
|
1.0
|
N
|
B:SER89
|
4.3
|
66.9
|
1.0
|
N
|
B:LYS127
|
4.3
|
72.0
|
1.0
|
O
|
B:LYS127
|
4.3
|
77.0
|
1.0
|
NH2
|
B:ARG85
|
4.5
|
53.1
|
1.0
|
C
|
B:ASP125
|
4.5
|
62.5
|
1.0
|
CA
|
B:SER89
|
4.5
|
68.0
|
1.0
|
C
|
B:LYS127
|
4.5
|
76.6
|
1.0
|
OD2
|
B:ASP125
|
4.5
|
73.3
|
1.0
|
CB
|
B:ASP125
|
4.6
|
64.1
|
1.0
|
CB
|
B:SER255
|
4.7
|
53.3
|
1.0
|
N
|
B:THR126
|
4.7
|
64.5
|
1.0
|
CA
|
B:THR126
|
4.8
|
66.9
|
1.0
|
|
Potassium binding site 3 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 3 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K604
b:86.3
occ:1.00
|
OD1
|
C:ASN87
|
2.4
|
54.5
|
1.0
|
OD1
|
C:ASP125
|
2.5
|
52.4
|
1.0
|
OG
|
C:SER89
|
2.7
|
58.0
|
1.0
|
O
|
C:THR126
|
2.8
|
47.5
|
1.0
|
CG
|
C:ASP125
|
3.4
|
50.4
|
1.0
|
CG
|
C:ASN87
|
3.5
|
52.7
|
1.0
|
OG
|
C:SER255
|
3.6
|
43.1
|
1.0
|
C
|
C:THR126
|
3.7
|
48.0
|
1.0
|
CB
|
C:SER89
|
3.7
|
55.1
|
1.0
|
O
|
C:ASP125
|
3.9
|
45.8
|
1.0
|
NZ
|
C:LYS282
|
3.9
|
39.9
|
1.0
|
ND2
|
C:ASN87
|
4.0
|
52.5
|
1.0
|
C
|
C:ASP125
|
4.1
|
45.4
|
1.0
|
N
|
C:SER89
|
4.1
|
52.8
|
1.0
|
CB
|
C:ASP125
|
4.1
|
44.8
|
1.0
|
NH2
|
C:ARG85
|
4.2
|
46.9
|
1.0
|
OD2
|
C:ASP125
|
4.2
|
53.3
|
1.0
|
CA
|
C:LYS127
|
4.3
|
52.9
|
1.0
|
N
|
C:LYS127
|
4.3
|
50.2
|
1.0
|
N
|
C:THR126
|
4.5
|
45.5
|
1.0
|
CA
|
C:SER89
|
4.5
|
53.8
|
1.0
|
CA
|
C:THR126
|
4.6
|
45.8
|
1.0
|
N
|
C:PHE88
|
4.7
|
50.4
|
1.0
|
O
|
C:LYS127
|
4.7
|
56.2
|
1.0
|
CB
|
C:ASN87
|
4.7
|
49.7
|
1.0
|
CA
|
C:ASP125
|
4.8
|
44.0
|
1.0
|
C
|
C:LYS127
|
4.8
|
55.3
|
1.0
|
CA
|
C:ASN87
|
4.8
|
49.5
|
1.0
|
CB
|
C:SER255
|
4.9
|
40.6
|
1.0
|
O4
|
C:OXL602
|
5.0
|
63.2
|
1.0
|
C
|
C:ASN87
|
5.0
|
50.7
|
1.0
|
|
Potassium binding site 4 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 4 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K604
b:57.0
occ:1.00
|
OD1
|
D:ASP125
|
2.5
|
44.7
|
1.0
|
OD1
|
D:ASN87
|
2.7
|
39.8
|
1.0
|
OG
|
D:SER89
|
2.7
|
43.6
|
1.0
|
O
|
D:THR126
|
2.7
|
44.1
|
1.0
|
O
|
D:HOH758
|
3.0
|
46.3
|
1.0
|
CG
|
D:ASP125
|
3.5
|
41.8
|
1.0
|
C
|
D:THR126
|
3.6
|
44.5
|
1.0
|
OG
|
D:SER255
|
3.6
|
40.4
|
1.0
|
CG
|
D:ASN87
|
3.8
|
38.7
|
1.0
|
O
|
D:ASP125
|
3.8
|
39.9
|
1.0
|
CB
|
D:SER89
|
3.9
|
40.3
|
1.0
|
NZ
|
D:LYS282
|
4.0
|
37.0
|
1.0
|
C
|
D:ASP125
|
4.1
|
39.4
|
1.0
|
N
|
D:SER89
|
4.1
|
38.1
|
1.0
|
CB
|
D:ASP125
|
4.2
|
37.5
|
1.0
|
CA
|
D:LYS127
|
4.3
|
50.3
|
1.0
|
N
|
D:LYS127
|
4.3
|
46.9
|
1.0
|
OD2
|
D:ASP125
|
4.3
|
42.6
|
1.0
|
NH2
|
D:ARG85
|
4.3
|
37.4
|
1.0
|
ND2
|
D:ASN87
|
4.3
|
38.9
|
1.0
|
N
|
D:THR126
|
4.4
|
40.0
|
1.0
|
CA
|
D:SER89
|
4.6
|
38.9
|
1.0
|
CA
|
D:THR126
|
4.6
|
41.3
|
1.0
|
O
|
D:LYS127
|
4.7
|
54.8
|
1.0
|
N
|
D:PHE88
|
4.7
|
36.4
|
1.0
|
CA
|
D:ASP125
|
4.7
|
37.6
|
1.0
|
C
|
D:LYS127
|
4.8
|
53.6
|
1.0
|
CB
|
D:SER255
|
4.9
|
38.9
|
1.0
|
CB
|
D:ASN87
|
4.9
|
35.6
|
1.0
|
O
|
D:HOH879
|
5.0
|
51.2
|
1.0
|
CA
|
D:ASN87
|
5.0
|
35.4
|
1.0
|
|
Potassium binding site 5 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 5 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K604
b:119.4
occ:1.00
|
OG
|
E:SER89
|
2.5
|
81.4
|
1.0
|
OD1
|
E:ASN87
|
2.6
|
68.9
|
1.0
|
O
|
E:THR126
|
2.6
|
74.7
|
1.0
|
OD1
|
E:ASP125
|
2.7
|
75.9
|
1.0
|
C
|
E:THR126
|
3.5
|
74.6
|
1.0
|
CB
|
E:SER89
|
3.6
|
78.4
|
1.0
|
OG
|
E:SER255
|
3.6
|
62.0
|
1.0
|
CG
|
E:ASN87
|
3.7
|
68.5
|
1.0
|
CG
|
E:ASP125
|
3.7
|
76.5
|
1.0
|
O
|
E:ASP125
|
3.9
|
71.2
|
1.0
|
CA
|
E:LYS127
|
4.0
|
78.4
|
1.0
|
N
|
E:SER89
|
4.0
|
75.5
|
1.0
|
NZ
|
E:LYS282
|
4.1
|
55.6
|
1.0
|
N
|
E:LYS127
|
4.1
|
76.3
|
1.0
|
C
|
E:ASP125
|
4.2
|
71.1
|
1.0
|
ND2
|
E:ASN87
|
4.2
|
69.1
|
1.0
|
CA
|
E:SER89
|
4.3
|
77.1
|
1.0
|
CB
|
E:ASP125
|
4.4
|
72.6
|
1.0
|
O
|
E:LYS127
|
4.5
|
80.2
|
1.0
|
N
|
E:THR126
|
4.5
|
71.3
|
1.0
|
NH2
|
E:ARG85
|
4.5
|
57.0
|
1.0
|
OD2
|
E:ASP125
|
4.5
|
79.4
|
1.0
|
C
|
E:LYS127
|
4.5
|
79.9
|
1.0
|
CA
|
E:THR126
|
4.6
|
72.4
|
1.0
|
N
|
E:PHE88
|
4.7
|
70.4
|
1.0
|
CB
|
E:SER255
|
4.8
|
61.3
|
1.0
|
CB
|
E:ASN87
|
4.9
|
66.5
|
1.0
|
CA
|
E:ASP125
|
4.9
|
70.7
|
1.0
|
C
|
E:PHE88
|
4.9
|
74.4
|
1.0
|
CA
|
E:ASN87
|
5.0
|
66.5
|
1.0
|
|
Potassium binding site 6 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 6 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K604
b:90.1
occ:1.00
|
OG
|
F:SER89
|
2.6
|
61.4
|
1.0
|
OD1
|
F:ASP125
|
2.6
|
63.1
|
1.0
|
O
|
F:THR126
|
2.7
|
56.7
|
1.0
|
OD1
|
F:ASN87
|
2.8
|
51.8
|
1.0
|
OG
|
F:SER255
|
3.4
|
45.9
|
1.0
|
C
|
F:THR126
|
3.6
|
56.3
|
1.0
|
CG
|
F:ASP125
|
3.6
|
60.3
|
1.0
|
CB
|
F:SER89
|
3.7
|
60.2
|
1.0
|
NZ
|
F:LYS282
|
3.8
|
39.2
|
1.0
|
CG
|
F:ASN87
|
3.8
|
51.9
|
1.0
|
O
|
F:ASP125
|
4.1
|
48.4
|
1.0
|
CA
|
F:LYS127
|
4.2
|
61.6
|
1.0
|
ND2
|
F:ASN87
|
4.2
|
52.4
|
1.0
|
N
|
F:LYS127
|
4.3
|
58.7
|
1.0
|
C
|
F:ASP125
|
4.3
|
49.6
|
1.0
|
N
|
F:SER89
|
4.3
|
59.5
|
1.0
|
OD2
|
F:ASP125
|
4.4
|
62.1
|
1.0
|
O
|
F:LYS127
|
4.4
|
64.1
|
1.0
|
NH2
|
F:ARG85
|
4.4
|
49.0
|
1.0
|
CB
|
F:ASP125
|
4.4
|
52.7
|
1.0
|
N
|
F:THR126
|
4.6
|
51.1
|
1.0
|
C
|
F:LYS127
|
4.6
|
63.5
|
1.0
|
CA
|
F:SER89
|
4.6
|
60.1
|
1.0
|
CB
|
F:SER255
|
4.6
|
46.0
|
1.0
|
CA
|
F:THR126
|
4.7
|
53.1
|
1.0
|
N
|
F:PHE88
|
5.0
|
55.8
|
1.0
|
|
Potassium binding site 7 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 7 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K604
b:74.5
occ:1.00
|
OD1
|
G:ASP125
|
2.6
|
49.9
|
1.0
|
O
|
G:THR126
|
2.6
|
42.4
|
1.0
|
OD1
|
G:ASN87
|
2.7
|
45.2
|
1.0
|
OG
|
G:SER89
|
2.7
|
53.3
|
1.0
|
O
|
G:HOH878
|
3.4
|
71.8
|
1.0
|
OG
|
G:SER255
|
3.5
|
42.1
|
1.0
|
C
|
G:THR126
|
3.6
|
43.2
|
1.0
|
CG
|
G:ASP125
|
3.6
|
47.2
|
1.0
|
CG
|
G:ASN87
|
3.8
|
44.5
|
1.0
|
NZ
|
G:LYS282
|
3.8
|
42.1
|
1.0
|
CB
|
G:SER89
|
3.8
|
49.9
|
1.0
|
O
|
G:HOH816
|
4.0
|
54.7
|
1.0
|
O
|
G:ASP125
|
4.0
|
39.5
|
1.0
|
CA
|
G:LYS127
|
4.1
|
47.6
|
1.0
|
N
|
G:LYS127
|
4.2
|
45.0
|
1.0
|
O
|
G:HOH899
|
4.2
|
60.0
|
1.0
|
ND2
|
G:ASN87
|
4.2
|
44.8
|
1.0
|
C
|
G:ASP125
|
4.2
|
39.6
|
1.0
|
N
|
G:SER89
|
4.3
|
47.0
|
1.0
|
CB
|
G:ASP125
|
4.4
|
40.4
|
1.0
|
OD2
|
G:ASP125
|
4.4
|
48.1
|
1.0
|
NH2
|
G:ARG85
|
4.4
|
48.1
|
1.0
|
O
|
G:LYS127
|
4.5
|
49.0
|
1.0
|
N
|
G:THR126
|
4.5
|
39.9
|
1.0
|
C
|
G:LYS127
|
4.6
|
48.9
|
1.0
|
CA
|
G:THR126
|
4.6
|
41.0
|
1.0
|
CA
|
G:SER89
|
4.6
|
48.3
|
1.0
|
CB
|
G:SER255
|
4.7
|
40.3
|
1.0
|
O2
|
G:OXL602
|
4.8
|
52.3
|
1.0
|
CA
|
G:ASP125
|
4.9
|
38.6
|
1.0
|
N
|
G:PHE88
|
4.9
|
43.9
|
1.0
|
CB
|
G:ASN87
|
5.0
|
43.5
|
1.0
|
|
Potassium binding site 8 out
of 8 in 5sci
Go back to
Potassium Binding Sites List in 5sci
Potassium binding site 8 out
of 8 in the Structure of Liver Pyruvate Kinase in Complex with Anthraquinone Derivative 105
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 105 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K604
b:64.9
occ:1.00
|
OD1
|
H:ASP125
|
2.5
|
42.2
|
1.0
|
OD1
|
H:ASN87
|
2.6
|
38.8
|
1.0
|
O
|
H:THR126
|
2.7
|
39.3
|
1.0
|
OG
|
H:SER89
|
2.9
|
43.0
|
1.0
|
CG
|
H:ASP125
|
3.5
|
40.8
|
1.0
|
C
|
H:THR126
|
3.6
|
40.0
|
1.0
|
OG
|
H:SER255
|
3.6
|
32.9
|
1.0
|
CG
|
H:ASN87
|
3.7
|
36.9
|
1.0
|
O
|
H:ASP125
|
3.9
|
34.2
|
1.0
|
NZ
|
H:LYS282
|
3.9
|
34.1
|
1.0
|
CB
|
H:SER89
|
4.0
|
40.8
|
1.0
|
C
|
H:ASP125
|
4.1
|
34.9
|
1.0
|
N
|
H:SER89
|
4.2
|
40.2
|
1.0
|
CB
|
H:ASP125
|
4.2
|
35.2
|
1.0
|
ND2
|
H:ASN87
|
4.2
|
36.4
|
1.0
|
N
|
H:LYS127
|
4.3
|
42.3
|
1.0
|
CA
|
H:LYS127
|
4.3
|
45.9
|
1.0
|
OD2
|
H:ASP125
|
4.3
|
42.8
|
1.0
|
NH2
|
H:ARG85
|
4.3
|
37.7
|
1.0
|
N
|
H:THR126
|
4.4
|
35.5
|
1.0
|
CA
|
H:THR126
|
4.6
|
37.2
|
1.0
|
CA
|
H:SER89
|
4.6
|
40.7
|
1.0
|
O
|
H:LYS127
|
4.7
|
48.0
|
1.0
|
N
|
H:PHE88
|
4.7
|
36.9
|
1.0
|
CB
|
H:SER255
|
4.7
|
33.3
|
1.0
|
C
|
H:LYS127
|
4.7
|
48.1
|
1.0
|
CA
|
H:ASP125
|
4.8
|
34.4
|
1.0
|
CB
|
H:ASN87
|
4.9
|
34.3
|
1.0
|
CA
|
H:ASN87
|
4.9
|
35.2
|
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
|