Zinc in PDB 4fgj: Oxidized Quinone Reductase 2 in Complex with Primaquine

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

The structure of Oxidized Quinone Reductase 2 in Complex with Primaquine, PDB code: 4fgj 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)	30.06 / 1.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.500, 83.000, 106.490, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 16.7

The binding sites of Zinc atom in the Oxidized Quinone Reductase 2 in Complex with Primaquine (pdb code 4fgj). 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 Primaquine, PDB code: 4fgj:
Jump to Zinc binding site number: 1; 2;

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


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 Primaquine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:18.4 occ:1.00 ND1 A:HIS173 2.0 15.9 1.0 ND1 A:HIS177 2.0 16.5 1.0 O A:CYS222 2.1 17.6 1.0 SG A:CYS222 2.3 18.6 1.0 HB3 A:CYS222 2.5 21.6 1.0 CB A:CYS222 2.8 18.0 1.0 C A:CYS222 2.9 18.1 1.0 HA A:HIS173 2.9 14.5 1.0 CE1 A:HIS173 2.9 16.0 1.0 CG A:HIS177 3.0 14.8 1.0 CE1 A:HIS177 3.0 16.5 1.0 HB2 A:HIS177 3.0 16.0 1.0 CG A:HIS173 3.1 14.3 1.0 HE1 A:HIS173 3.1 19.2 1.0 HB3 A:HIS177 3.1 16.0 1.0 HB2 A:HIS173 3.2 15.2 1.0 HE1 A:HIS177 3.2 19.8 1.0 CB A:HIS177 3.2 13.3 1.0 CA A:CYS222 3.4 17.3 1.0 CB A:HIS173 3.4 12.7 1.0 HB2 A:CYS222 3.6 21.6 1.0 CA A:HIS173 3.6 12.1 1.0 HA A:CYS222 3.9 20.8 1.0 N A:THR223 4.0 18.1 1.0 NE2 A:HIS173 4.1 15.3 1.0 HA A:THR223 4.1 21.5 1.0 NE2 A:HIS177 4.1 16.6 1.0 CD2 A:HIS177 4.1 15.2 1.0 CD2 A:HIS173 4.2 14.7 1.0 HE1 A:HIS227 4.2 17.1 1.0 O A:HOH541 4.4 35.5 1.0 HB3 A:HIS173 4.4 15.2 1.0 HE1 A:TYR132 4.5 16.8 1.0 N A:CYS222 4.5 17.4 1.0 CA A:THR223 4.6 17.9 1.0 HD1 A:TYR132 4.6 16.4 1.0 HZ3 A:TRP169 4.6 16.2 1.0 H A:CYS222 4.6 20.9 1.0 N A:HIS173 4.6 11.6 1.0 C A:HIS173 4.6 10.5 1.0 H A:THR223 4.6 21.8 1.0 O A:HIS173 4.6 12.3 1.0 O A:GLN172 4.7 12.1 1.0 CA A:HIS177 4.8 12.4 1.0 HE2 A:HIS173 4.8 18.4 1.0 HE2 A:HIS177 4.9 19.9 1.0 CE1 A:HIS227 4.9 14.3 1.0 C A:GLN172 5.0 10.6 1.0 HD2 A:HIS177 5.0 18.3 1.0

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


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 Primaquine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:8.5 occ:1.00 ND1 B:HIS173 2.0 8.0 1.0 O B:CYS222 2.0 8.1 1.0 ND1 B:HIS177 2.1 8.4 1.0 SG B:CYS222 2.3 7.8 1.0 HB3 B:CYS222 2.6 9.4 1.0 CB B:CYS222 2.9 7.8 1.0 HA B:HIS173 2.9 6.5 1.0 C B:CYS222 2.9 8.5 1.0 CE1 B:HIS173 2.9 8.0 1.0 CG B:HIS177 3.0 6.9 1.0 CE1 B:HIS177 3.1 8.5 1.0 CG B:HIS173 3.1 7.2 1.0 HE1 B:HIS173 3.1 9.7 1.0 HB2 B:HIS177 3.1 6.4 1.0 HB3 B:HIS177 3.2 6.4 1.0 HB2 B:HIS173 3.2 7.8 1.0 HE1 B:HIS177 3.2 10.2 1.0 CB B:HIS177 3.3 5.3 1.0 CA B:CYS222 3.4 8.2 1.0 CB B:HIS173 3.4 6.5 1.0 CA B:HIS173 3.6 5.5 1.0 HB2 B:CYS222 3.7 9.4 1.0 HA B:CYS222 4.0 9.9 1.0 N B:THR223 4.0 9.4 1.0 HA B:THR223 4.1 11.5 1.0 NE2 B:HIS173 4.1 8.9 1.0 CD2 B:HIS173 4.2 8.2 1.0 NE2 B:HIS177 4.2 8.2 1.0 CD2 B:HIS177 4.2 7.3 1.0 HE1 B:HIS227 4.3 7.4 1.0 HB3 B:HIS173 4.4 7.8 1.0 N B:HIS173 4.5 5.0 1.0 CA B:THR223 4.6 9.6 1.0 N B:CYS222 4.6 8.7 1.0 C B:HIS173 4.6 5.2 1.0 HE1 B:TYR132 4.6 9.0 1.0 H B:CYS222 4.6 10.4 1.0 O B:HIS173 4.6 5.8 1.0 HZ3 B:TRP169 4.6 11.4 1.0 O B:GLN172 4.6 5.5 1.0 H B:THR223 4.7 11.3 1.0 HD1 B:TYR132 4.7 9.3 1.0 HE2 B:HIS173 4.8 10.7 1.0 CA B:HIS177 4.9 4.7 1.0 C B:GLN172 4.9 5.4 1.0 HE2 B:HIS177 4.9 9.9 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