Zinc in PDB 4zvm: Oxidized Quinone Reductase 2 in Complex with Doxorubicin

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

The structure of Oxidized Quinone Reductase 2 in Complex with Doxorubicin, PDB code: 4zvm 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)	15.54 / 1.97
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.230, 83.340, 106.620, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 22.9

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

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


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 Doxorubicin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:31.5 occ:1.00 ND1 A:HIS177 2.1 40.5 1.0 ND1 A:HIS173 2.2 26.5 1.0 SG A:CYS222 2.2 28.3 1.0 O A:CYS222 2.2 30.1 1.0 HB3 A:CYS222 2.7 50.4 1.0 HB2 A:HIS177 2.9 37.2 1.0 CG A:HIS177 2.9 36.7 1.0 CB A:CYS222 2.9 42.0 1.0 HB3 A:HIS177 3.0 37.2 1.0 HA A:HIS173 3.0 27.5 1.0 CE1 A:HIS173 3.1 28.8 1.0 C A:CYS222 3.1 34.1 1.0 CE1 A:HIS177 3.1 39.6 1.0 CB A:HIS177 3.1 31.0 1.0 CG A:HIS173 3.1 28.6 1.0 HB2 A:HIS173 3.1 27.9 1.0 HE1 A:HIS173 3.2 34.5 1.0 HE1 A:HIS177 3.4 47.6 1.0 CB A:HIS173 3.5 23.3 1.0 CA A:CYS222 3.6 37.2 1.0 CA A:HIS173 3.7 22.9 1.0 HB2 A:CYS222 3.8 50.4 1.0 CD2 A:HIS177 4.0 41.8 1.0 NE2 A:HIS177 4.1 48.3 1.0 HA A:CYS222 4.1 44.7 1.0 HD1 A:TYR132 4.2 35.3 1.0 NE2 A:HIS173 4.2 23.9 1.0 N A:THR223 4.2 40.2 1.0 HA A:THR223 4.2 51.8 1.0 CD2 A:HIS173 4.2 25.4 1.0 HE1 A:TYR132 4.3 36.0 1.0 HB3 A:HIS173 4.4 27.9 1.0 HE1 A:HIS227 4.4 42.6 1.0 O A:HIS173 4.6 22.3 1.0 C A:HIS173 4.6 19.7 1.0 CA A:HIS177 4.7 25.9 1.0 H A:CYS222 4.7 44.7 1.0 HZ3 A:TRP169 4.7 30.3 1.0 N A:CYS222 4.7 37.3 1.0 N A:HIS173 4.7 19.0 1.0 CA A:THR223 4.7 43.1 1.0 CD1 A:TYR132 4.8 29.4 1.0 O A:GLN172 4.8 20.1 1.0 CE1 A:TYR132 4.8 29.9 1.0 HD2 A:HIS177 4.8 50.2 1.0 H A:THR223 4.9 48.3 1.0 HE2 A:HIS177 4.9 58.0 1.0 HE2 A:HIS173 4.9 28.7 1.0 H A:HIS177 5.0 32.3 1.0

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


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 Doxorubicin within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:22.5 occ:1.00 ND1 B:HIS173 2.0 19.9 1.0 O B:CYS222 2.1 22.1 1.0 ND1 B:HIS177 2.1 26.6 1.0 SG B:CYS222 2.2 17.6 1.0 HB3 B:CYS222 2.5 21.4 1.0 CB B:CYS222 2.8 17.8 1.0 HA B:HIS173 2.9 20.5 1.0 C B:CYS222 2.9 23.1 1.0 CE1 B:HIS173 3.0 21.4 1.0 CG B:HIS173 3.0 20.8 1.0 HB2 B:HIS177 3.1 20.0 1.0 HB2 B:HIS173 3.1 21.6 1.0 CG B:HIS177 3.1 19.2 1.0 HB3 B:HIS177 3.1 20.0 1.0 CE1 B:HIS177 3.2 22.0 1.0 HE1 B:HIS173 3.2 25.7 1.0 CB B:HIS177 3.3 16.7 1.0 HE1 B:HIS177 3.4 26.4 1.0 CB B:HIS173 3.4 18.0 1.0 CA B:CYS222 3.4 20.4 1.0 CA B:HIS173 3.6 17.1 1.0 HB2 B:CYS222 3.7 21.4 1.0 HA B:CYS222 3.9 24.5 1.0 N B:THR223 4.0 21.8 1.0 NE2 B:HIS173 4.1 16.9 1.0 HA B:THR223 4.2 22.9 1.0 CD2 B:HIS173 4.2 15.7 1.0 CD2 B:HIS177 4.2 26.8 1.0 HE1 B:HIS227 4.3 23.5 1.0 NE2 B:HIS177 4.3 27.2 1.0 HB3 B:HIS173 4.3 21.6 1.0 HE1 B:TYR132 4.5 20.4 1.0 N B:HIS173 4.5 13.5 1.0 N B:CYS222 4.6 20.3 1.0 C B:HIS173 4.6 15.7 1.0 H B:CYS222 4.6 24.3 1.0 CA B:THR223 4.6 19.0 1.0 O B:HIS173 4.6 13.5 1.0 O B:GLN172 4.7 13.8 1.0 HD1 B:TYR132 4.7 25.3 1.0 H B:THR223 4.7 26.2 1.0 HZ3 B:TRP169 4.7 24.0 1.0 CA B:HIS177 4.8 13.2 1.0 HE2 B:HIS173 4.9 20.3 1.0 C B:GLN172 4.9 15.8 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