Chlorine in PDB 4fgl: Reduced Quinone Reductase 2 in Complex with Chloroquine
Enzymatic activity of Reduced Quinone Reductase 2 in Complex with Chloroquine
All present enzymatic activity of Reduced Quinone Reductase 2 in Complex with Chloroquine:
1.10.99.2;
Protein crystallography data
The structure of Reduced Quinone Reductase 2 in Complex with Chloroquine, PDB code: 4fgl
was solved by
K.K.Leung,
B.H.Shilton,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
48.31 /
1.20
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
54.310,
105.710,
82.000,
90.00,
90.17,
90.00
|
|
R / Rfree (%)
|
15.9 /
17.3
|
Other elements in 4fgl:
The structure of Reduced Quinone Reductase 2 in Complex with Chloroquine also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Reduced Quinone Reductase 2 in Complex with Chloroquine
(pdb code 4fgl). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the
Reduced Quinone Reductase 2 in Complex with Chloroquine, PDB code: 4fgl:
Jump to Chlorine binding site number:
1;
2;
3;
4;
5;
Chlorine binding site 1 out
of 5 in 4fgl
Go back to
Chlorine Binding Sites List in 4fgl
Chlorine binding site 1 out
of 5 in the Reduced Quinone Reductase 2 in Complex with Chloroquine
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cl303
b:19.6
occ:1.00
|
CL
|
A:CLQ303
|
0.0
|
19.6
|
1.0
|
|
C7
|
A:CLQ303
|
1.7
|
17.8
|
1.0
|
|
HD22
|
A:ASN161
|
2.6
|
12.3
|
1.0
|
|
C8
|
A:CLQ303
|
2.7
|
17.7
|
1.0
|
|
C6
|
A:CLQ303
|
2.7
|
14.1
|
1.0
|
|
H81
|
A:CLQ303
|
2.8
|
21.2
|
1.0
|
|
H61
|
A:CLQ303
|
2.8
|
16.9
|
1.0
|
|
HE1
|
B:PHE178
|
2.8
|
9.8
|
1.0
|
|
HE1
|
A:PHE106
|
3.0
|
9.3
|
1.0
|
|
OD1
|
A:ASN161
|
3.1
|
9.3
|
1.0
|
|
ND2
|
A:ASN161
|
3.2
|
10.2
|
1.0
|
|
CE1
|
B:PHE178
|
3.3
|
8.2
|
1.0
|
|
HN3
|
A:FAD302
|
3.5
|
5.8
|
1.0
|
|
O
|
A:HOH452
|
3.5
|
9.4
|
1.0
|
|
CG
|
A:ASN161
|
3.5
|
8.3
|
1.0
|
|
N3
|
A:FAD302
|
3.8
|
4.9
|
1.0
|
|
HE2
|
A:MET154
|
3.8
|
20.8
|
1.0
|
|
CD1
|
B:PHE178
|
3.9
|
7.3
|
1.0
|
|
HD1
|
B:PHE178
|
3.9
|
8.8
|
1.0
|
|
HD21
|
A:ASN161
|
3.9
|
12.3
|
1.0
|
|
OH
|
A:TYR155
|
3.9
|
6.8
|
1.0
|
|
CZ
|
B:PHE178
|
3.9
|
7.8
|
1.0
|
|
CE1
|
A:PHE106
|
3.9
|
7.8
|
1.0
|
|
HZ
|
B:PHE178
|
4.0
|
9.3
|
1.0
|
|
C5
|
A:CLQ303
|
4.0
|
11.0
|
1.0
|
|
C9
|
A:CLQ303
|
4.0
|
11.9
|
1.0
|
|
O2
|
A:FAD302
|
4.2
|
5.5
|
1.0
|
|
C2
|
A:FAD302
|
4.2
|
5.5
|
1.0
|
|
HE1
|
A:MET154
|
4.2
|
20.8
|
1.0
|
|
HH
|
B:TYR132
|
4.3
|
8.8
|
1.0
|
|
HA3
|
A:GLY150
|
4.4
|
8.7
|
1.0
|
|
HH
|
A:TYR155
|
4.4
|
8.1
|
1.0
|
|
C4
|
A:FAD302
|
4.5
|
4.6
|
1.0
|
|
CE
|
A:MET154
|
4.5
|
17.4
|
1.0
|
|
HZ
|
A:PHE106
|
4.5
|
9.1
|
1.0
|
|
C4
|
A:CLQ303
|
4.5
|
16.0
|
1.0
|
|
CZ
|
A:TYR155
|
4.6
|
7.0
|
1.0
|
|
OH
|
B:TYR132
|
4.6
|
7.4
|
1.0
|
|
O4
|
A:FAD302
|
4.7
|
5.3
|
1.0
|
|
CZ
|
A:PHE106
|
4.7
|
7.6
|
1.0
|
|
HE2
|
B:TYR132
|
4.7
|
9.4
|
1.0
|
|
HD1
|
A:PHE106
|
4.7
|
8.5
|
1.0
|
|
H51
|
A:CLQ303
|
4.7
|
13.2
|
1.0
|
|
CB
|
A:ASN161
|
4.8
|
7.6
|
1.0
|
|
CD1
|
A:PHE106
|
4.8
|
7.1
|
1.0
|
|
H
|
A:GLY150
|
4.9
|
7.0
|
1.0
|
|
HB3
|
A:ASN161
|
4.9
|
9.0
|
1.0
|
|
CG
|
B:PHE178
|
4.9
|
5.4
|
1.0
|
|
CE2
|
B:PHE178
|
4.9
|
7.1
|
1.0
|
|
Chlorine binding site 2 out
of 5 in 4fgl
Go back to
Chlorine Binding Sites List in 4fgl
Chlorine binding site 2 out
of 5 in the Reduced Quinone Reductase 2 in Complex with Chloroquine
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 2 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cl303
b:22.5
occ:1.00
|
CL
|
B:CLQ303
|
0.0
|
22.5
|
1.0
|
|
C7
|
B:CLQ303
|
1.7
|
16.1
|
1.0
|
|
HD22
|
B:ASN161
|
2.5
|
12.9
|
1.0
|
|
C8
|
B:CLQ303
|
2.7
|
15.0
|
1.0
|
|
C6
|
B:CLQ303
|
2.7
|
17.3
|
1.0
|
|
H81
|
B:CLQ303
|
2.8
|
18.0
|
1.0
|
|
H61
|
B:CLQ303
|
2.8
|
20.8
|
1.0
|
|
HE1
|
A:PHE178
|
3.1
|
8.7
|
1.0
|
|
ND2
|
B:ASN161
|
3.2
|
10.8
|
1.0
|
|
OD1
|
B:ASN161
|
3.3
|
10.8
|
1.0
|
|
HE1
|
B:PHE106
|
3.4
|
11.2
|
1.0
|
|
HN3
|
B:FAD302
|
3.5
|
8.5
|
1.0
|
|
CG
|
B:ASN161
|
3.6
|
9.1
|
1.0
|
|
CE1
|
A:PHE178
|
3.7
|
7.2
|
1.0
|
|
HE1
|
B:MET154
|
3.7
|
18.7
|
1.0
|
|
HE2
|
B:MET154
|
3.7
|
18.7
|
1.0
|
|
HD21
|
B:ASN161
|
3.8
|
12.9
|
1.0
|
|
OH
|
B:TYR155
|
3.8
|
7.8
|
1.0
|
|
N3
|
B:FAD302
|
3.9
|
7.1
|
1.0
|
|
O
|
B:HOH439
|
3.9
|
10.8
|
1.0
|
|
O2
|
B:FAD302
|
3.9
|
7.2
|
1.0
|
|
C9
|
B:CLQ303
|
4.0
|
13.1
|
1.0
|
|
C5
|
B:CLQ303
|
4.0
|
21.9
|
1.0
|
|
CE
|
B:MET154
|
4.1
|
15.6
|
1.0
|
|
C2
|
B:FAD302
|
4.1
|
6.2
|
1.0
|
|
HA3
|
B:GLY150
|
4.2
|
10.8
|
1.0
|
|
HZ
|
A:PHE178
|
4.3
|
10.3
|
1.0
|
|
CZ
|
A:PHE178
|
4.3
|
8.6
|
1.0
|
|
CE1
|
B:PHE106
|
4.3
|
9.3
|
1.0
|
|
HD1
|
A:PHE178
|
4.3
|
8.0
|
1.0
|
|
CD1
|
A:PHE178
|
4.3
|
6.7
|
1.0
|
|
HE3
|
B:MET154
|
4.3
|
18.7
|
1.0
|
|
HH
|
B:TYR155
|
4.3
|
9.4
|
1.0
|
|
CZ
|
B:TYR155
|
4.5
|
7.3
|
1.0
|
|
C4
|
B:CLQ303
|
4.5
|
17.6
|
1.0
|
|
H
|
B:GLY150
|
4.6
|
9.4
|
1.0
|
|
C4
|
B:FAD302
|
4.7
|
5.9
|
1.0
|
|
H51
|
B:CLQ303
|
4.8
|
26.2
|
1.0
|
|
HZ
|
B:PHE106
|
4.8
|
10.1
|
1.0
|
|
HE2
|
B:TYR155
|
4.8
|
10.0
|
1.0
|
|
OH
|
A:TYR132
|
4.9
|
8.6
|
1.0
|
|
CA
|
B:GLY150
|
4.9
|
9.0
|
1.0
|
|
HE2
|
A:TYR132
|
4.9
|
8.8
|
1.0
|
|
HA2
|
B:GLY150
|
4.9
|
10.8
|
1.0
|
|
CB
|
B:ASN161
|
4.9
|
8.7
|
1.0
|
|
CE2
|
B:TYR155
|
4.9
|
8.4
|
1.0
|
|
N
|
B:GLY150
|
5.0
|
7.8
|
1.0
|
|
O4
|
B:FAD302
|
5.0
|
6.3
|
1.0
|
|
Chlorine binding site 3 out
of 5 in 4fgl
Go back to
Chlorine Binding Sites List in 4fgl
Chlorine binding site 3 out
of 5 in the Reduced Quinone Reductase 2 in Complex with Chloroquine
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 3 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cl303
b:21.0
occ:1.00
|
CL
|
C:CLQ303
|
0.0
|
21.0
|
1.0
|
|
C7
|
C:CLQ303
|
1.7
|
13.2
|
1.0
|
|
HE1
|
C:MET154
|
2.6
|
25.2
|
1.0
|
|
C8
|
C:CLQ303
|
2.7
|
13.6
|
1.0
|
|
C6
|
C:CLQ303
|
2.7
|
13.7
|
1.0
|
|
H61
|
C:CLQ303
|
2.8
|
16.4
|
1.0
|
|
H81
|
C:CLQ303
|
2.8
|
16.3
|
1.0
|
|
HD22
|
C:ASN161
|
2.9
|
15.2
|
1.0
|
|
HE2
|
C:MET154
|
3.0
|
25.2
|
1.0
|
|
O
|
C:HOH557
|
3.1
|
19.3
|
1.0
|
|
HA2
|
C:GLY150
|
3.2
|
13.8
|
1.0
|
|
CE
|
C:MET154
|
3.3
|
21.1
|
1.0
|
|
HA3
|
C:GLY150
|
3.3
|
13.8
|
1.0
|
|
CA
|
C:GLY150
|
3.5
|
11.5
|
1.0
|
|
HE1
|
D:PHE178
|
3.6
|
13.7
|
1.0
|
|
N
|
C:GLY150
|
3.6
|
10.8
|
1.0
|
|
H
|
C:GLY150
|
3.6
|
12.9
|
1.0
|
|
ND2
|
C:ASN161
|
3.8
|
12.7
|
1.0
|
|
HE3
|
C:MET154
|
3.9
|
25.2
|
1.0
|
|
C5
|
C:CLQ303
|
4.0
|
14.4
|
1.0
|
|
C9
|
C:CLQ303
|
4.0
|
12.6
|
1.0
|
|
O2
|
C:FAD302
|
4.1
|
8.6
|
1.0
|
|
HZ
|
D:PHE178
|
4.1
|
14.5
|
1.0
|
|
HD21
|
C:ASN161
|
4.2
|
15.2
|
1.0
|
|
O
|
C:HOH567
|
4.2
|
29.8
|
1.0
|
|
C
|
C:GLY149
|
4.3
|
8.8
|
1.0
|
|
C2
|
C:FAD302
|
4.3
|
7.9
|
1.0
|
|
CE1
|
D:PHE178
|
4.3
|
11.4
|
1.0
|
|
HD12
|
D:ILE128
|
4.4
|
20.8
|
1.0
|
|
HA3
|
C:GLY149
|
4.5
|
10.5
|
1.0
|
|
C4
|
C:CLQ303
|
4.5
|
13.1
|
1.0
|
|
SD
|
C:MET154
|
4.5
|
16.6
|
1.0
|
|
CZ
|
D:PHE178
|
4.6
|
12.1
|
1.0
|
|
OD1
|
C:ASN161
|
4.7
|
12.0
|
1.0
|
|
CG
|
C:ASN161
|
4.7
|
11.2
|
1.0
|
|
N3
|
C:FAD302
|
4.7
|
7.8
|
1.0
|
|
HN3
|
C:FAD302
|
4.7
|
9.3
|
1.0
|
|
H51
|
C:CLQ303
|
4.7
|
17.3
|
1.0
|
|
N1
|
C:FAD302
|
4.8
|
8.9
|
1.0
|
|
O
|
C:GLY149
|
4.8
|
11.2
|
1.0
|
|
HH
|
C:TYR155
|
4.8
|
11.4
|
1.0
|
|
CA
|
C:GLY149
|
5.0
|
8.8
|
1.0
|
|
Chlorine binding site 4 out
of 5 in 4fgl
Go back to
Chlorine Binding Sites List in 4fgl
Chlorine binding site 4 out
of 5 in the Reduced Quinone Reductase 2 in Complex with Chloroquine
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 4 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl303
b:14.0
occ:1.00
|
CL
|
D:CLQ303
|
0.0
|
14.0
|
1.0
|
|
C7
|
D:CLQ303
|
1.7
|
9.1
|
1.0
|
|
C6
|
D:CLQ303
|
2.7
|
10.5
|
1.0
|
|
C8
|
D:CLQ303
|
2.7
|
10.8
|
1.0
|
|
HE1
|
D:MET154
|
2.7
|
23.8
|
1.0
|
|
H61
|
D:CLQ303
|
2.8
|
12.6
|
1.0
|
|
H81
|
D:CLQ303
|
2.8
|
13.0
|
1.0
|
|
HD22
|
D:ASN161
|
3.0
|
12.4
|
1.0
|
|
HA2
|
D:GLY150
|
3.3
|
9.8
|
1.0
|
|
HA3
|
D:GLY150
|
3.3
|
9.8
|
1.0
|
|
HE2
|
D:MET154
|
3.3
|
23.8
|
1.0
|
|
CE
|
D:MET154
|
3.4
|
19.9
|
1.0
|
|
HE2
|
C:PHE178
|
3.5
|
9.3
|
1.0
|
|
CA
|
D:GLY150
|
3.6
|
8.2
|
1.0
|
|
H
|
D:GLY150
|
3.7
|
10.7
|
1.0
|
|
N
|
D:GLY150
|
3.7
|
8.9
|
1.0
|
|
ND2
|
D:ASN161
|
3.8
|
10.4
|
1.0
|
|
O2
|
D:FAD302
|
3.9
|
6.7
|
1.0
|
|
HZ
|
C:PHE178
|
3.9
|
10.2
|
1.0
|
|
C5
|
D:CLQ303
|
4.0
|
10.6
|
1.0
|
|
C9
|
D:CLQ303
|
4.0
|
8.7
|
1.0
|
|
HD21
|
D:ASN161
|
4.1
|
12.4
|
1.0
|
|
HE3
|
D:MET154
|
4.1
|
23.8
|
1.0
|
|
CE2
|
C:PHE178
|
4.2
|
7.8
|
1.0
|
|
C2
|
D:FAD302
|
4.2
|
7.4
|
1.0
|
|
HH
|
D:TYR155
|
4.4
|
9.1
|
1.0
|
|
C
|
D:GLY149
|
4.4
|
8.8
|
1.0
|
|
CZ
|
C:PHE178
|
4.4
|
8.5
|
1.0
|
|
HD12
|
C:ILE128
|
4.4
|
10.6
|
1.0
|
|
O
|
D:HOH522
|
4.5
|
24.4
|
1.0
|
|
C4
|
D:CLQ303
|
4.5
|
9.8
|
1.0
|
|
SD
|
D:MET154
|
4.5
|
12.8
|
1.0
|
|
HN3
|
D:FAD302
|
4.5
|
8.0
|
1.0
|
|
N3
|
D:FAD302
|
4.6
|
6.7
|
1.0
|
|
HA3
|
D:GLY149
|
4.6
|
9.2
|
1.0
|
|
H51
|
D:CLQ303
|
4.7
|
12.7
|
1.0
|
|
N1
|
D:FAD302
|
4.7
|
6.8
|
1.0
|
|
OH
|
D:TYR155
|
4.7
|
7.6
|
1.0
|
|
CG
|
D:ASN161
|
4.9
|
7.5
|
1.0
|
|
O
|
D:GLY149
|
4.9
|
10.2
|
1.0
|
|
HE2
|
D:TYR155
|
5.0
|
9.8
|
1.0
|
|
HE2
|
C:PHE131
|
5.0
|
10.8
|
1.0
|
|
CE2
|
C:PHE131
|
5.0
|
9.0
|
1.0
|
|
Chlorine binding site 5 out
of 5 in 4fgl
Go back to
Chlorine Binding Sites List in 4fgl
Chlorine binding site 5 out
of 5 in the Reduced Quinone Reductase 2 in Complex with Chloroquine
 Mono view
 Stereo pair view
|
|
A full contact list of Chlorine with other atoms in the Cl binding
site number 5 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cl304
b:18.7
occ:1.00
|
CL
|
D:CLQ304
|
0.0
|
18.7
|
1.0
|
|
C7
|
D:CLQ304
|
1.7
|
13.3
|
1.0
|
|
C6
|
D:CLQ304
|
2.7
|
19.6
|
1.0
|
|
C8
|
D:CLQ304
|
2.7
|
19.5
|
1.0
|
|
HG21
|
D:VAL26
|
2.7
|
11.3
|
1.0
|
|
H61
|
D:CLQ304
|
2.8
|
23.5
|
1.0
|
|
H81
|
D:CLQ304
|
2.8
|
23.4
|
1.0
|
|
HG11
|
D:VAL26
|
2.9
|
14.2
|
1.0
|
|
HB
|
D:VAL26
|
3.1
|
11.6
|
1.0
|
|
HZ2
|
D:LYS22
|
3.1
|
14.8
|
1.0
|
|
HA
|
D:ASN23
|
3.2
|
12.4
|
1.0
|
|
HZ3
|
D:LYS22
|
3.2
|
14.8
|
1.0
|
|
CG2
|
D:VAL26
|
3.4
|
9.4
|
1.0
|
|
OD1
|
D:ASN23
|
3.4
|
12.4
|
1.0
|
|
O
|
D:HOH455
|
3.5
|
13.9
|
1.0
|
|
HD2
|
D:LYS22
|
3.5
|
15.0
|
1.0
|
|
CB
|
D:VAL26
|
3.5
|
9.7
|
1.0
|
|
NZ
|
D:LYS22
|
3.6
|
12.3
|
1.0
|
|
CG1
|
D:VAL26
|
3.6
|
11.9
|
1.0
|
|
HG23
|
D:VAL26
|
3.8
|
11.3
|
1.0
|
|
HD3
|
D:LYS22
|
3.8
|
15.0
|
1.0
|
|
C5
|
D:CLQ304
|
4.0
|
21.7
|
1.0
|
|
C9
|
D:CLQ304
|
4.0
|
19.5
|
1.0
|
|
CD
|
D:LYS22
|
4.1
|
12.5
|
1.0
|
|
HG12
|
D:VAL26
|
4.1
|
14.2
|
1.0
|
|
CG
|
D:ASN23
|
4.1
|
12.6
|
1.0
|
|
HG22
|
D:VAL26
|
4.2
|
11.3
|
1.0
|
|
CA
|
D:ASN23
|
4.2
|
10.3
|
1.0
|
|
HZ1
|
D:LYS22
|
4.3
|
14.8
|
1.0
|
|
HG13
|
D:VAL26
|
4.4
|
14.2
|
1.0
|
|
HG21
|
D:VAL38
|
4.5
|
12.1
|
1.0
|
|
C4
|
D:CLQ304
|
4.5
|
20.0
|
1.0
|
|
CE
|
D:LYS22
|
4.5
|
11.4
|
1.0
|
|
CB
|
D:ASN23
|
4.6
|
10.4
|
1.0
|
|
HB3
|
D:ASN23
|
4.6
|
12.5
|
1.0
|
|
H51
|
D:CLQ304
|
4.7
|
26.0
|
1.0
|
|
O
|
D:ASN23
|
4.8
|
11.5
|
1.0
|
|
O
|
D:LYS22
|
4.9
|
8.9
|
1.0
|
|
N
|
D:ASN23
|
4.9
|
8.9
|
1.0
|
|
Reference:
K.K.Leung,
B.H.Shilton.
Crystal Structures of Quinone Reductase 2 Bound to Antimalarial Drugs Reveal Conformational Change Upon Reduction J.Biol.Chem. 2013.
ISSN: ESSN 1083-351X
Page generated: Sun Jul 21 13:44:38 2024
|
