Zinc 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:

Chlorine

(Cl)

3 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Oxidized Quinone Reductase 2 in Complex with Chloroquine, PDB code: 4fgk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Oxidized Quinone Reductase 2 in Complex with Chloroquine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn 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:Zn303 b:22.3 occ:1.00 ND1 A:HIS173 2.0 18.1 1.0 O A:CYS222 2.1 21.3 1.0 ND1 A:HIS177 2.1 21.4 1.0 SG A:CYS222 2.3 20.4 1.0 HB3 A:CYS222 2.4 28.6 1.0 CB A:CYS222 2.7 23.8 1.0 C A:CYS222 2.9 26.3 1.0 HA A:HIS173 2.9 17.0 1.0 CE1 A:HIS173 2.9 22.2 1.0 CG A:HIS177 3.0 22.3 1.0 HB2 A:HIS177 3.1 23.1 1.0 CG A:HIS173 3.1 17.6 1.0 HE1 A:HIS173 3.1 26.6 1.0 HB3 A:HIS177 3.1 23.1 1.0 CE1 A:HIS177 3.1 20.1 1.0 HB2 A:HIS173 3.2 18.5 1.0 CB A:HIS177 3.3 19.3 1.0 HE1 A:HIS177 3.3 24.1 1.0 CA A:CYS222 3.3 23.0 1.0 CB A:HIS173 3.4 15.4 1.0 HB2 A:CYS222 3.6 28.6 1.0 CA A:HIS173 3.7 14.2 1.0 HA A:CYS222 3.8 27.6 1.0 N A:THR223 4.0 24.2 1.0 NE2 A:HIS173 4.1 19.1 1.0 HA A:THR223 4.1 27.5 1.0 CD2 A:HIS173 4.2 16.3 1.0 CD2 A:HIS177 4.2 22.4 1.0 NE2 A:HIS177 4.2 25.2 1.0 HE1 A:HIS227 4.2 21.6 1.0 O A:HOH557 4.3 45.2 1.0 HE1 A:TYR132 4.3 16.9 0.6 HD1 A:TYR132 4.4 16.5 0.6 HB3 A:HIS173 4.4 18.5 1.0 N A:CYS222 4.5 24.4 1.0 H A:CYS222 4.6 29.3 1.0 CA A:THR223 4.6 22.9 1.0 HZ3 A:TRP169 4.6 24.6 1.0 N A:HIS173 4.6 14.2 1.0 H A:THR223 4.6 29.1 1.0 C A:HIS173 4.6 11.8 1.0 O A:HIS173 4.7 14.6 1.0 O A:GLN172 4.7 17.3 1.0 CE1 A:TYR132 4.8 14.1 0.6 CA A:HIS177 4.8 18.6 1.0 CD1 A:TYR132 4.8 13.8 0.6 HE2 A:HIS173 4.8 22.9 1.0 O A:HOH611 4.9 31.8 1.0 CE1 A:HIS227 5.0 18.0 1.0 C A:GLN172 5.0 12.9 1.0 HE2 A:HIS177 5.0 30.3 1.0

Zinc binding site 2 out of 2 in the Oxidized Quinone Reductase 2 in Complex with Chloroquine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Oxidized Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:11.7 occ:1.00 ND1 B:HIS173 2.0 11.4 1.0 O B:CYS222 2.0 11.8 1.0 ND1 B:HIS177 2.1 13.4 1.0 SG B:CYS222 2.3 11.5 1.0 HB3 B:CYS222 2.6 15.2 1.0 CB B:CYS222 2.9 12.7 1.0 C B:CYS222 2.9 11.7 1.0 HA B:HIS173 2.9 11.9 1.0 CE1 B:HIS173 2.9 14.1 1.0 CG B:HIS177 3.0 10.7 1.0 CG B:HIS173 3.0 11.7 1.0 CE1 B:HIS177 3.1 13.4 1.0 HE1 B:HIS173 3.1 16.9 1.0 HB2 B:HIS177 3.1 11.6 1.0 HB3 B:HIS177 3.1 11.6 1.0 HB2 B:HIS173 3.1 12.5 1.0 HE1 B:HIS177 3.3 16.1 1.0 CB B:HIS177 3.3 9.7 1.0 CB B:HIS173 3.4 10.4 1.0 CA B:CYS222 3.4 12.5 1.0 CA B:HIS173 3.6 9.9 1.0 HB2 B:CYS222 3.7 15.2 1.0 HA B:CYS222 4.0 15.0 1.0 N B:THR223 4.0 12.7 1.0 NE2 B:HIS173 4.1 13.0 1.0 HA B:THR223 4.1 15.3 1.0 CD2 B:HIS173 4.1 11.6 1.0 NE2 B:HIS177 4.2 12.7 1.0 CD2 B:HIS177 4.2 10.2 1.0 HE1 B:HIS227 4.3 12.6 1.0 HB3 B:HIS173 4.4 12.5 1.0 HE1 B:TYR132 4.5 12.8 1.0 N B:HIS173 4.6 9.1 1.0 N B:CYS222 4.6 12.6 1.0 CA B:THR223 4.6 12.8 1.0 H B:CYS222 4.6 15.1 1.0 HZ3 B:TRP169 4.6 16.5 1.0 C B:HIS173 4.6 10.9 1.0 HD1 B:TYR132 4.6 13.9 1.0 O B:HIS173 4.6 10.3 1.0 O B:GLN172 4.7 9.4 1.0 H B:THR223 4.7 15.3 1.0 O B:HOH561 4.8 37.5 1.0 HE2 B:HIS173 4.8 15.6 1.0 CA B:HIS177 4.8 9.3 1.0 C B:GLN172 4.9 9.9 1.0 HE2 B:HIS177 4.9 15.2 1.0 HD2 B:HIS173 5.0 13.9 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