Zinc in PDB 4fgl: 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;

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

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

Chlorine

(Cl)

5 atoms

The binding sites of Zinc 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 Zinc atom.
In total 4 binding sites of Zinc where determined in the Reduced Quinone Reductase 2 in Complex with Chloroquine, PDB code: 4fgl:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Reduced 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 Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:6.5 occ:1.00 ND1 A:HIS173 2.0 7.2 1.0 ND1 A:HIS177 2.0 5.7 1.0 O A:CYS222 2.0 6.8 1.0 SG A:CYS222 2.2 6.5 1.0 HB3 A:CYS222 2.6 7.2 1.0 CB A:CYS222 2.9 6.0 1.0 HA A:HIS173 2.9 6.8 1.0 C A:CYS222 2.9 5.8 1.0 CE1 A:HIS173 2.9 6.9 1.0 CE1 A:HIS177 3.0 7.4 1.0 CG A:HIS177 3.0 5.2 1.0 CG A:HIS173 3.1 5.6 1.0 HE1 A:HIS173 3.1 8.3 1.0 HB2 A:HIS177 3.1 7.0 1.0 HE1 A:HIS177 3.2 8.8 1.0 HB3 A:HIS177 3.2 7.0 1.0 HB2 A:HIS173 3.2 8.4 1.0 CB A:HIS177 3.3 5.9 1.0 CA A:CYS222 3.4 6.4 1.0 CB A:HIS173 3.5 7.0 1.0 CA A:HIS173 3.6 5.7 1.0 HB2 A:CYS222 3.7 7.2 1.0 HA A:CYS222 4.0 7.6 1.0 N A:THR223 4.0 5.7 1.0 NE2 A:HIS173 4.1 7.9 1.0 NE2 A:HIS177 4.1 7.1 1.0 HA A:THR223 4.1 7.0 1.0 CD2 A:HIS173 4.2 7.3 1.0 CD2 A:HIS177 4.2 6.6 1.0 HE1 A:HIS227 4.3 8.2 1.0 HB3 A:HIS173 4.4 8.4 1.0 O A:HOH570 4.5 19.6 1.0 HZ3 A:TRP169 4.5 8.8 1.0 N A:HIS173 4.5 5.6 1.0 N A:CYS222 4.6 6.9 1.0 H A:CYS222 4.6 8.2 1.0 HE1 A:TYR132 4.6 9.1 1.0 CA A:THR223 4.6 5.9 1.0 O A:GLN172 4.6 5.8 1.0 C A:HIS173 4.6 4.8 1.0 HD1 A:TYR132 4.7 7.3 1.0 O A:HIS173 4.7 5.9 1.0 H A:THR223 4.7 6.9 1.0 O A:HOH447 4.8 12.0 1.0 HE2 A:HIS173 4.8 9.5 1.0 CA A:HIS177 4.9 5.5 1.0 HE2 A:HIS177 4.9 8.5 1.0 C A:GLN172 4.9 5.5 1.0 O A:HOH449 5.0 10.7 1.0 CZ3 A:TRP169 5.0 7.3 1.0

Zinc binding site 2 out of 4 in the Reduced 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 Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:7.2 occ:1.00 O B:CYS222 2.0 7.7 1.0 ND1 B:HIS173 2.0 5.9 1.0 ND1 B:HIS177 2.0 7.7 1.0 SG B:CYS222 2.3 7.5 1.0 HB3 B:CYS222 2.6 8.4 1.0 CB B:CYS222 2.8 7.0 1.0 C B:CYS222 2.9 7.4 1.0 HA B:HIS173 2.9 7.1 1.0 CE1 B:HIS173 2.9 6.5 1.0 CE1 B:HIS177 3.0 7.9 1.0 CG B:HIS177 3.0 7.5 1.0 CG B:HIS173 3.0 5.6 1.0 HE1 B:HIS173 3.1 7.8 1.0 HB2 B:HIS177 3.1 7.9 1.0 HB3 B:HIS177 3.1 7.9 1.0 HB2 B:HIS173 3.2 7.8 1.0 HE1 B:HIS177 3.2 9.4 1.0 CB B:HIS177 3.3 6.6 1.0 CA B:CYS222 3.4 6.1 1.0 CB B:HIS173 3.4 6.5 1.0 CA B:HIS173 3.6 5.9 1.0 HB2 B:CYS222 3.7 8.4 1.0 HA B:CYS222 4.0 7.3 1.0 N B:THR223 4.0 7.8 1.0 NE2 B:HIS173 4.1 7.3 1.0 HA B:THR223 4.1 10.3 1.0 NE2 B:HIS177 4.1 8.4 1.0 CD2 B:HIS173 4.1 7.2 1.0 CD2 B:HIS177 4.2 7.3 1.0 HE1 B:HIS227 4.3 7.8 1.0 HB3 B:HIS173 4.4 7.8 1.0 HE1 B:TYR132 4.4 7.8 1.0 N B:CYS222 4.5 9.1 1.0 N B:HIS173 4.5 5.8 1.0 H B:CYS222 4.5 10.9 1.0 HZ3 B:TRP169 4.6 8.0 1.0 CA B:THR223 4.6 8.6 1.0 HD1 B:TYR132 4.6 9.1 1.0 C B:HIS173 4.6 5.4 1.0 O B:GLN172 4.6 6.5 1.0 O B:HIS173 4.7 5.5 1.0 H B:THR223 4.7 9.3 1.0 CA B:HIS177 4.8 6.5 1.0 HE2 B:HIS173 4.8 8.7 1.0 C B:GLN172 4.9 5.3 1.0 HE2 B:HIS177 4.9 10.1 1.0 O B:HOH481 5.0 14.2 1.0 CE1 B:TYR132 5.0 6.6 1.0 CZ3 B:TRP169 5.0 6.7 1.0

Zinc binding site 3 out of 4 in the Reduced 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 3 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:7.5 occ:1.00 O C:CYS222 2.0 8.0 1.0 ND1 C:HIS173 2.0 6.9 1.0 ND1 C:HIS177 2.0 6.6 1.0 SG C:CYS222 2.2 7.3 1.0 HB3 C:CYS222 2.6 10.0 1.0 CB C:CYS222 2.8 8.4 1.0 HA C:HIS173 2.8 9.0 1.0 C C:CYS222 2.9 8.8 1.0 CE1 C:HIS173 3.0 7.3 1.0 CE1 C:HIS177 3.0 6.7 1.0 CG C:HIS177 3.0 6.3 1.0 CG C:HIS173 3.1 7.4 1.0 HB3 C:HIS177 3.1 7.1 1.0 HE1 C:HIS173 3.1 8.7 1.0 HB2 C:HIS173 3.2 7.8 1.0 HB2 C:HIS177 3.2 7.1 1.0 HE1 C:HIS177 3.2 8.0 1.0 CB C:HIS177 3.3 6.0 1.0 CA C:CYS222 3.4 8.6 1.0 CB C:HIS173 3.4 6.5 1.0 CA C:HIS173 3.6 7.5 1.0 HB2 C:CYS222 3.7 10.0 1.0 HA C:CYS222 3.9 10.3 1.0 N C:THR223 4.0 9.8 1.0 HA C:THR223 4.1 13.7 1.0 NE2 C:HIS173 4.1 8.6 1.0 NE2 C:HIS177 4.1 7.8 1.0 CD2 C:HIS177 4.1 6.4 1.0 CD2 C:HIS173 4.2 7.1 1.0 HE1 C:HIS227 4.3 9.7 1.0 HE1 C:TYR132 4.3 8.3 1.0 HB3 C:HIS173 4.4 7.8 1.0 N C:HIS173 4.5 6.4 1.0 HZ3 C:TRP169 4.5 11.4 1.0 CA C:THR223 4.6 11.4 1.0 N C:CYS222 4.6 9.7 1.0 C C:HIS173 4.6 6.4 1.0 H C:CYS222 4.6 11.6 1.0 O C:HIS173 4.6 6.2 1.0 O C:GLN172 4.6 6.7 1.0 H C:THR223 4.6 11.7 1.0 HD1 C:TYR132 4.6 7.5 1.0 CA C:HIS177 4.8 6.0 1.0 HE2 C:HIS173 4.9 10.3 1.0 CE1 C:TYR132 4.9 6.9 1.0 C C:GLN172 4.9 5.8 1.0 HE2 C:HIS177 4.9 9.3 1.0 CZ3 C:TRP169 5.0 9.5 1.0 HD2 C:HIS177 5.0 7.7 1.0

Zinc binding site 4 out of 4 in the Reduced 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 4 of Reduced Quinone Reductase 2 in Complex with Chloroquine within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn301 b:7.2 occ:1.00 O D:CYS222 2.0 7.5 1.0 ND1 D:HIS173 2.0 6.1 1.0 ND1 D:HIS177 2.0 8.1 1.0 SG D:CYS222 2.3 6.6 1.0 HB3 D:CYS222 2.7 5.9 1.0 C D:CYS222 2.9 6.5 1.0 CB D:CYS222 2.9 4.9 1.0 HA D:HIS173 2.9 9.0 1.0 CE1 D:HIS173 2.9 7.1 1.0 CG D:HIS177 3.0 7.2 1.0 CE1 D:HIS177 3.0 8.8 1.0 CG D:HIS173 3.0 6.0 1.0 HB2 D:HIS177 3.1 8.6 1.0 HB2 D:HIS173 3.1 8.8 1.0 HE1 D:HIS173 3.1 8.5 1.0 HB3 D:HIS177 3.1 8.6 1.0 HE1 D:HIS177 3.2 10.5 1.0 CB D:HIS177 3.3 7.2 1.0 CB D:HIS173 3.4 7.3 1.0 CA D:CYS222 3.4 6.7 1.0 CA D:HIS173 3.6 7.5 1.0 HB2 D:CYS222 3.8 5.9 1.0 HA D:CYS222 4.0 8.1 1.0 N D:THR223 4.0 6.2 1.0 HA D:THR223 4.0 9.8 1.0 NE2 D:HIS173 4.1 7.5 1.0 NE2 D:HIS177 4.1 9.0 1.0 CD2 D:HIS173 4.1 7.0 1.0 CD2 D:HIS177 4.2 7.7 1.0 HE1 D:HIS227 4.3 8.8 1.0 HB3 D:HIS173 4.3 8.8 1.0 O C:HOH576 4.4 23.9 1.0 HE1 D:TYR132 4.4 9.1 1.0 HZ3 D:TRP169 4.5 10.1 1.0 CA D:THR223 4.5 8.1 1.0 N D:CYS222 4.5 7.2 1.0 H D:CYS222 4.6 8.6 1.0 N D:HIS173 4.6 6.2 1.0 HD1 D:TYR132 4.6 10.7 1.0 C D:HIS173 4.6 6.5 1.0 O D:HIS173 4.6 7.2 1.0 H D:THR223 4.6 7.4 1.0 O D:GLN172 4.6 6.6 1.0 CA D:HIS177 4.8 7.8 1.0 HE2 D:HIS173 4.9 9.0 1.0 HE2 D:HIS177 4.9 10.7 1.0 C D:GLN172 4.9 6.8 1.0 CE1 D:TYR132 5.0 7.6 1.0 CZ3 D:TRP169 5.0 8.5 1.0 O D:HOH421 5.0 11.8 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