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Chlorine in PDB 4fgk: Oxidized Quinone Reductase 2 in Complex with Chloroquine

Enzymatic activity of Oxidized Quinone Reductase 2 in Complex with Chloroquine

All present enzymatic activity of Oxidized Quinone Reductase 2 in Complex with Chloroquine:
1.10.99.2;

Protein crystallography data

The structure of Oxidized Quinone Reductase 2 in Complex with Chloroquine, PDB code: 4fgk 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) 32.67 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.370, 83.110, 106.580, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 17.4

Other elements in 4fgk:

The structure of Oxidized Quinone Reductase 2 in Complex with Chloroquine also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Oxidized Quinone Reductase 2 in Complex with Chloroquine (pdb code 4fgk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Oxidized Quinone Reductase 2 in Complex with Chloroquine, PDB code: 4fgk:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 4fgk

Go back to Chlorine Binding Sites List in 4fgk
Chlorine binding site 1 out of 3 in the Oxidized 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 Oxidized Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:14.5
occ:0.48
CL A:0TX302 0.0 14.5 0.5
C7 A:0TX302 1.7 8.2 0.5
C6 A:0TX302 2.3 21.1 0.5
CL A:0TX302 2.3 27.7 0.5
C7 A:0TX302 2.7 25.2 0.5
C6 A:0TX302 2.7 10.7 0.5
C8 A:0TX302 2.7 15.3 0.5
HZ A:PHE126 2.8 35.7 1.0
HE1 A:PHE126 3.0 32.9 1.0
C6 B:FAD302 3.3 11.4 1.0
CZ A:PHE126 3.3 29.7 1.0
CE1 A:PHE126 3.4 27.4 1.0
C5X B:FAD302 3.5 10.2 1.0
O A:HOH440 3.5 17.4 1.0
H6 B:FAD302 3.5 13.7 1.0
C7 B:FAD302 3.5 10.6 1.0
C5 A:0TX302 3.6 22.1 0.5
HZ2 B:TRP105 3.7 14.6 1.0
CZ2 B:TRP105 3.8 12.2 1.0
O A:HOH460 3.8 22.6 1.0
C9A B:FAD302 3.9 12.3 1.0
C8 B:FAD302 3.9 13.2 1.0
N5 B:FAD302 4.0 12.5 1.0
C5 A:0TX302 4.0 13.1 0.5
C9 A:0TX302 4.0 10.1 0.5
HM71 B:FAD302 4.0 13.4 1.0
C8 A:0TX302 4.1 21.6 0.5
C9 B:FAD302 4.1 12.8 1.0
CE2 B:TRP105 4.1 11.1 1.0
C7M B:FAD302 4.2 11.2 1.0
CH2 B:TRP105 4.3 16.5 1.0
HM72 B:FAD302 4.4 13.4 1.0
HE1 B:TRP105 4.4 13.8 1.0
NE1 B:TRP105 4.4 11.5 1.0
CE2 A:PHE126 4.5 29.7 1.0
C4 A:0TX302 4.5 12.8 0.5
HH2 B:TRP105 4.5 19.9 1.0
O A:LEU120 4.6 13.4 1.0
HM82 B:FAD302 4.6 14.8 1.0
CD1 A:PHE126 4.6 27.7 1.0
O A:HOH473 4.6 23.1 1.0
N10 B:FAD302 4.7 11.7 1.0
C4 A:0TX302 4.7 21.9 0.5
H9 B:FAD302 4.7 15.3 1.0
C4X B:FAD302 4.8 11.7 1.0
CD2 B:TRP105 4.8 9.6 1.0
HE2 A:PHE126 4.8 35.6 1.0
HB3 A:GLN122 4.9 29.8 0.6
HA A:CYS121 4.9 17.8 1.0
C8M B:FAD302 4.9 12.3 1.0
C9 A:0TX302 4.9 20.9 0.5
H A:GLN122 4.9 22.6 0.4
H A:GLN122 4.9 26.7 0.6
HE2 A:PHE178 5.0 25.3 1.0
HB2 A:GLN122 5.0 14.9 0.4
CZ3 B:TRP105 5.0 15.5 1.0

Chlorine binding site 2 out of 3 in 4fgk

Go back to Chlorine Binding Sites List in 4fgk
Chlorine binding site 2 out of 3 in the Oxidized 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 Oxidized Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:27.7
occ:0.52
CL A:0TX302 0.0 27.7 0.5
C8 A:0TX302 0.4 15.3 0.5
C7 A:0TX302 1.0 8.2 0.5
C9 A:0TX302 1.7 10.1 0.5
C7 A:0TX302 1.7 25.2 0.5
C6 A:0TX302 2.1 10.7 0.5
CL A:0TX302 2.3 14.5 0.5
C4 A:0TX302 2.5 12.8 0.5
C5 A:0TX302 2.6 13.1 0.5
C6 A:0TX302 2.7 21.1 0.5
C8 A:0TX302 2.7 21.6 0.5
N1 A:0TX302 2.8 13.8 0.5
N5 B:FAD302 3.1 12.5 1.0
C5X B:FAD302 3.5 10.2 1.0
C4X B:FAD302 3.5 11.7 1.0
CH2 B:TRP105 3.6 16.5 1.0
CZ3 B:TRP105 3.6 15.5 1.0
CZ2 B:TRP105 3.7 12.2 1.0
HE2 A:PHE178 3.8 25.3 1.0
CE3 B:TRP105 3.8 14.8 1.0
C3 A:0TX302 3.9 15.0 0.5
C6 B:FAD302 3.9 11.4 1.0
H6 B:FAD302 3.9 13.7 1.0
HH2 B:TRP105 3.9 19.9 1.0
CE2 B:TRP105 3.9 11.1 1.0
HZ A:PHE126 3.9 35.7 1.0
C5 A:0TX302 4.0 22.1 0.5
C9 A:0TX302 4.0 20.9 0.5
C1 A:0TX302 4.0 11.6 0.5
HZ3 B:TRP105 4.0 18.6 1.0
CD2 B:TRP105 4.0 9.6 1.0
C4 B:FAD302 4.0 11.2 1.0
H B:TRP105 4.1 11.7 1.0
CZ A:PHE126 4.1 29.7 1.0
O4 B:FAD302 4.1 12.3 1.0
C9A B:FAD302 4.1 12.3 1.0
HE1 A:PHE126 4.1 32.9 1.0
CE2 A:PHE178 4.1 21.1 1.0
HZ2 B:TRP105 4.2 14.6 1.0
C10 B:FAD302 4.2 13.0 1.0
CE1 A:PHE126 4.2 27.4 1.0
HE3 B:TRP105 4.3 17.8 1.0
C2 A:0TX302 4.4 13.8 0.5
HA B:TRP105 4.4 10.4 1.0
N10 B:FAD302 4.4 11.7 1.0
C4 A:0TX302 4.5 21.9 0.5
HD2 A:PHE178 4.5 20.5 1.0
CD2 A:PHE178 4.6 17.1 1.0
NE1 B:TRP105 4.7 11.5 1.0
CZ A:PHE178 4.8 25.4 1.0
C7 B:FAD302 4.8 10.6 1.0
CE2 A:PHE126 4.8 29.7 1.0
CG B:TRP105 4.8 10.6 1.0
N B:TRP105 4.9 9.7 1.0
HZ A:PHE178 4.9 30.4 1.0
N3 B:FAD302 4.9 11.6 1.0
N2 A:0TX302 5.0 15.8 0.5
HD11 A:ILE128 5.0 20.5 0.4
CD1 A:PHE126 5.0 27.7 1.0

Chlorine binding site 3 out of 3 in 4fgk

Go back to Chlorine Binding Sites List in 4fgk
Chlorine binding site 3 out of 3 in the Oxidized 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 Oxidized Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl304

b:31.2
occ:0.83
CL A:0TX304 0.0 31.2 0.8
C7 A:0TX304 1.7 28.3 1.0
O B:HOH689 2.4 46.5 1.0
C6 A:0TX304 2.7 26.8 1.0
C8 A:0TX304 2.7 27.4 1.0
H61 A:0TX304 2.8 32.1 1.0
H81 A:0TX304 2.8 32.8 1.0
N5 A:FAD301 3.2 9.1 1.0
CZ3 A:TRP105 3.3 11.3 1.0
CH2 A:TRP105 3.5 10.3 1.0
HZ3 A:TRP105 3.5 13.5 1.0
O A:HOH449 3.6 18.8 1.0
C4X A:FAD301 3.6 8.9 1.0
C5X A:FAD301 3.6 9.6 1.0
HE2 B:PHE178 3.6 15.5 1.0
HH2 A:TRP105 3.7 12.4 1.0
CE3 A:TRP105 3.7 9.1 1.0
CE2 B:PHE178 3.8 12.9 1.0
CZ2 A:TRP105 3.9 8.9 1.0
C5 A:0TX304 4.0 28.5 1.0
C9 A:0TX304 4.0 31.4 0.9
C4 A:FAD301 4.0 9.0 1.0
HE3 A:TRP105 4.1 11.0 1.0
C6 A:FAD301 4.1 9.3 1.0
HZ B:PHE126 4.1 21.1 1.0
H6 A:FAD301 4.1 11.2 1.0
O4 A:FAD301 4.1 12.0 1.0
CD2 A:TRP105 4.1 8.9 1.0
CZ B:PHE126 4.2 17.6 1.0
CE2 A:TRP105 4.2 8.0 1.0
CZ B:PHE178 4.2 13.5 1.0
C10 A:FAD301 4.2 10.0 1.0
CD2 B:PHE178 4.3 10.6 1.0
CE1 B:PHE126 4.3 15.4 1.0
C9A A:FAD301 4.3 10.2 1.0
HE1 B:PHE126 4.3 18.5 1.0
H A:TRP105 4.3 10.2 1.0
HZ B:PHE178 4.3 16.2 1.0
O B:HOH649 4.4 31.2 1.0
HD2 B:PHE178 4.4 12.7 1.0
HZ2 A:TRP105 4.4 10.7 1.0
C4 A:0TX304 4.5 32.7 0.8
N10 A:FAD301 4.6 10.6 1.0
HA A:TRP105 4.6 9.3 1.0
CE2 B:PHE126 4.7 17.1 1.0
H51 A:0TX304 4.7 34.2 1.0
N3 A:FAD301 4.9 11.7 1.0
CD1 B:PHE126 4.9 13.9 1.0
HE2 B:PHE126 5.0 20.5 1.0
CE1 B:PHE178 5.0 13.1 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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