Zinc in PDB 4zvk: Reduced Quinone Reductase 2 in Complex with Ethidium

All present enzymatic activity of Reduced Quinone Reductase 2 in Complex with Ethidium:
1.10.99.2;

The structure of Reduced Quinone Reductase 2 in Complex with Ethidium, PDB code: 4zvk 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)	16.27 / 1.87
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.020, 82.570, 106.250, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 19.9

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

Zinc binding site 1 out of 2 in the Reduced Quinone Reductase 2 in Complex with Ethidium


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 Ethidium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:20.8 occ:1.00 ND1 A:HIS177 2.1 24.5 1.0 ND1 A:HIS173 2.1 17.9 1.0 O A:CYS222 2.1 23.8 1.0 SG A:CYS222 2.2 15.7 1.0 HB3 A:CYS222 2.5 19.8 1.0 CB A:CYS222 2.8 16.5 1.0 HA A:HIS173 2.9 20.3 1.0 C A:CYS222 2.9 22.5 1.0 CE1 A:HIS173 3.0 19.6 1.0 CG A:HIS177 3.0 20.3 1.0 CE1 A:HIS177 3.1 22.5 1.0 HE1 A:HIS173 3.1 23.5 1.0 HB2 A:HIS177 3.1 18.2 1.0 CG A:HIS173 3.1 14.7 1.0 HB3 A:HIS177 3.1 18.2 1.0 HE1 A:HIS177 3.3 27.0 1.0 CB A:HIS177 3.3 15.2 1.0 HB2 A:HIS173 3.3 21.7 1.0 CA A:CYS222 3.4 18.1 1.0 CB A:HIS173 3.5 18.1 1.0 HB2 A:CYS222 3.6 19.8 1.0 CA A:HIS173 3.6 16.9 1.0 HA A:CYS222 3.9 21.7 1.0 N A:THR223 4.0 27.2 1.0 NE2 A:HIS173 4.1 19.0 1.0 NE2 A:HIS177 4.2 21.4 1.0 CD2 A:HIS177 4.2 22.2 1.0 HA A:THR223 4.2 22.5 1.0 CD2 A:HIS173 4.2 17.9 1.0 HE1 A:TYR132 4.3 23.3 1.0 HE1 A:HIS227 4.3 26.2 1.0 HB3 A:HIS173 4.5 21.7 1.0 HD1 A:TYR132 4.5 21.3 1.0 N A:CYS222 4.5 23.4 1.0 HZ3 A:TRP169 4.6 25.7 1.0 N A:HIS173 4.6 13.0 1.0 H A:CYS222 4.6 28.1 1.0 O A:GLN172 4.6 16.7 1.0 C A:HIS173 4.6 14.2 1.0 CA A:THR223 4.6 18.8 1.0 O A:HIS173 4.6 19.2 1.0 H A:THR223 4.7 32.6 1.0 CA A:HIS177 4.8 16.6 1.0 HE2 A:HIS173 4.9 22.8 1.0 CE1 A:TYR132 4.9 19.4 1.0 C A:GLN172 4.9 20.4 1.0 HE2 A:HIS177 4.9 25.7 1.0

Zinc binding site 2 out of 2 in the Reduced Quinone Reductase 2 in Complex with Ethidium


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 Ethidium within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:20.4 occ:1.00 ND1 B:HIS173 2.0 17.1 1.0 ND1 B:HIS177 2.1 18.2 1.0 O B:CYS222 2.1 18.0 1.0 SG B:CYS222 2.3 18.2 1.0 HB3 B:CYS222 2.6 27.8 1.0 CB B:CYS222 2.8 23.1 1.0 HA B:HIS173 2.9 20.6 1.0 CE1 B:HIS173 3.0 17.4 1.0 C B:CYS222 3.0 23.2 1.0 HB2 B:HIS177 3.0 15.3 1.0 CG B:HIS177 3.0 20.9 1.0 HB3 B:HIS177 3.1 15.3 1.0 CG B:HIS173 3.1 20.4 1.0 HE1 B:HIS173 3.1 20.9 1.0 CE1 B:HIS177 3.2 19.2 1.0 HB2 B:HIS173 3.2 23.1 1.0 CB B:HIS177 3.2 12.7 1.0 HE1 B:HIS177 3.4 23.1 1.0 CA B:CYS222 3.5 20.8 1.0 CB B:HIS173 3.5 19.3 1.0 CA B:HIS173 3.6 17.2 1.0 HB2 B:CYS222 3.7 27.8 1.0 HA B:CYS222 4.0 25.0 1.0 N B:THR223 4.1 22.0 1.0 NE2 B:HIS173 4.1 15.3 1.0 HA B:THR223 4.1 22.1 1.0 CD2 B:HIS173 4.2 14.2 1.0 CD2 B:HIS177 4.2 19.3 1.0 NE2 B:HIS177 4.3 17.9 1.0 HE1 B:HIS227 4.3 20.4 1.0 HB3 B:HIS173 4.4 23.1 1.0 HE1 B:TYR132 4.4 16.9 1.0 N B:HIS173 4.6 12.2 1.0 N B:CYS222 4.6 20.8 1.0 HD1 B:TYR132 4.6 14.9 1.0 H B:CYS222 4.6 24.9 1.0 C B:HIS173 4.6 13.8 1.0 O B:GLN172 4.6 13.1 1.0 CA B:THR223 4.6 18.5 1.0 O B:HIS173 4.6 13.9 1.0 HZ3 B:TRP169 4.6 20.6 1.0 H B:THR223 4.7 26.4 1.0 CA B:HIS177 4.8 17.0 1.0 HE2 B:HIS173 4.9 18.3 1.0 C B:GLN172 4.9 12.3 1.0

K.K.Leung, B.H.Shilton. Binding of Dna-Intercalating Agents to Oxidized and Reduced Quinone Reductase 2. Biochemistry V. 54 7438 2015.
ISSN: ISSN 0006-2960
PubMed: 26636353
DOI: 10.1021/ACS.BIOCHEM.5B00884