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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:

Zinc (Zn) 4 atoms

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: Sat Dec 12 10:37:07 2020

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