Zinc in PDB 5buc: Oxidized Quinone Reductase 2 in Complex with Ethidium

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

The structure of Oxidized Quinone Reductase 2 in Complex with Ethidium, PDB code: 5buc 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)	13.01 / 1.87
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.810, 82.850, 106.430, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 19.9

The binding sites of Zinc atom in the Oxidized Quinone Reductase 2 in Complex with Ethidium (pdb code 5buc). 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 Ethidium, PDB code: 5buc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Oxidized 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 Oxidized Quinone Reductase 2 in Complex with Ethidium within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:18.9 occ:1.00 ND1 A:HIS173 2.0 18.6 1.0 ND1 A:HIS177 2.1 17.9 1.0 O A:CYS222 2.1 21.3 1.0 SG A:CYS222 2.2 17.5 1.0 CB A:CYS222 2.8 16.8 1.0 CE1 A:HIS173 3.0 17.3 1.0 C A:CYS222 3.0 19.7 1.0 CG A:HIS177 3.0 15.1 1.0 CG A:HIS173 3.0 16.7 1.0 CE1 A:HIS177 3.1 19.4 1.0 CB A:HIS177 3.2 10.6 1.0 CB A:HIS173 3.4 13.9 1.0 CA A:CYS222 3.4 20.0 1.0 CA A:HIS173 3.6 15.0 1.0 N A:THR223 4.1 23.7 1.0 NE2 A:HIS173 4.1 18.4 1.0 CD2 A:HIS177 4.1 18.8 1.0 CD2 A:HIS173 4.2 14.0 1.0 NE2 A:HIS177 4.2 18.8 1.0 O A:HOH544 4.3 35.4 1.0 N A:HIS173 4.6 14.0 1.0 C A:HIS173 4.6 13.3 1.0 N A:CYS222 4.6 20.8 1.0 O A:HIS173 4.6 14.1 1.0 CA A:THR223 4.6 19.5 1.0 H A:CYS222 4.6 24.9 1.0 O A:GLN172 4.6 13.8 1.0 H A:THR223 4.7 28.4 1.0 CA A:HIS177 4.8 14.5 1.0 HE2 A:HIS173 4.9 22.1 1.0 CE1 A:TYR132 4.9 18.8 1.0 C A:GLN172 4.9 16.5 1.0 HE2 A:HIS177 5.0 22.6 1.0 CD1 A:TYR132 5.0 16.2 1.0

Zinc binding site 2 out of 2 in the Oxidized 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 Oxidized Quinone Reductase 2 in Complex with Ethidium within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:18.4 occ:1.00 ND1 B:HIS173 2.0 13.1 1.0 ND1 B:HIS177 2.1 17.7 1.0 O B:CYS222 2.1 19.8 1.0 SG B:CYS222 2.3 17.0 1.0 CB B:CYS222 2.8 14.8 1.0 C B:CYS222 3.0 20.5 1.0 CE1 B:HIS173 3.0 14.8 1.0 CG B:HIS177 3.0 17.1 1.0 CG B:HIS173 3.1 15.9 1.0 CE1 B:HIS177 3.1 15.3 1.0 CB B:HIS177 3.3 12.8 1.0 CB B:HIS173 3.4 13.5 1.0 CA B:CYS222 3.5 15.7 1.0 CA B:HIS173 3.6 12.1 1.0 N B:THR223 4.1 20.6 1.0 NE2 B:HIS173 4.1 12.9 1.0 CD2 B:HIS173 4.2 11.5 1.0 CD2 B:HIS177 4.2 17.4 1.0 NE2 B:HIS177 4.2 17.8 1.0 N B:HIS173 4.5 10.2 1.0 N B:CYS222 4.6 17.2 1.0 C B:HIS173 4.6 10.7 1.0 CA B:THR223 4.6 15.8 1.0 H B:CYS222 4.6 20.6 1.0 O B:GLN172 4.6 11.9 1.0 O B:HIS173 4.7 12.7 1.0 H B:THR223 4.7 24.8 1.0 CA B:HIS177 4.8 12.1 1.0 HE2 B:HIS173 4.9 15.5 1.0 C B:GLN172 4.9 11.5 1.0 HE2 B:HIS177 5.0 21.3 1.0

K.K.Leung, B.H.Shilton. Structure of Quinone Reductase 2 in Complex with Dna Intercalating Agents To Be Published.