Chlorine in PDB 4fgk: 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;

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

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

Zinc

(Zn)

2 atoms

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 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 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 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

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