Zinc in PDB 2qwx: Crystal Structure of Quinone Reductase II

All present enzymatic activity of Crystal Structure of Quinone Reductase II:
1.10.99.2;

The structure of Crystal Structure of Quinone Reductase II, PDB code: 2qwx was solved by B.Calamini, B.D.Santarsiero, J.A.Boutin, A.D.Mesecar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.635, 83.549, 106.352, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 21.3

The binding sites of Zinc atom in the Crystal Structure of Quinone Reductase II (pdb code 2qwx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Quinone Reductase II, PDB code: 2qwx:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Quinone Reductase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Quinone Reductase II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn231 b:23.9 occ:1.00 ND1 A:HIS173 2.1 21.7 1.0 O A:CYS222 2.1 21.5 1.0 ND1 A:HIS177 2.1 23.2 1.0 SG A:CYS222 2.3 23.4 1.0 CB A:CYS222 2.8 25.3 1.0 C A:CYS222 3.0 24.4 1.0 CE1 A:HIS173 3.0 22.7 1.0 CG A:HIS177 3.1 19.9 1.0 CG A:HIS173 3.1 20.1 1.0 CE1 A:HIS177 3.1 21.4 1.0 CB A:HIS177 3.3 15.9 1.0 CA A:CYS222 3.4 24.0 1.0 CB A:HIS173 3.5 18.4 1.0 CA A:HIS173 3.6 16.7 1.0 N A:THR223 4.1 24.2 1.0 NE2 A:HIS173 4.1 21.5 1.0 CD2 A:HIS173 4.2 20.8 1.0 CD2 A:HIS177 4.2 21.7 1.0 NE2 A:HIS177 4.2 21.4 1.0 N A:HIS173 4.5 16.0 1.0 CA A:THR223 4.6 24.1 1.0 C A:HIS173 4.6 16.2 1.0 N A:CYS222 4.6 25.0 1.0 O A:HIS173 4.6 15.8 1.0 O A:GLN172 4.6 16.1 1.0 CA A:HIS177 4.9 15.5 1.0 C A:GLN172 4.9 15.0 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Quinone Reductase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Quinone Reductase II within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn231 b:35.2 occ:1.00 ND1 B:HIS177 2.1 29.8 1.0 ND1 B:HIS173 2.2 26.6 1.0 O B:CYS222 2.3 38.5 1.0 SG B:CYS222 2.4 32.6 1.0 CB B:CYS222 2.6 37.6 1.0 C B:CYS222 2.9 38.7 1.0 CG B:HIS177 3.0 27.8 1.0 CE1 B:HIS173 3.1 27.1 1.0 CE1 B:HIS177 3.1 29.1 1.0 CG B:HIS173 3.2 25.1 1.0 CA B:CYS222 3.3 38.5 1.0 CB B:HIS177 3.3 24.0 1.0 CB B:HIS173 3.5 23.3 1.0 CA B:HIS173 3.7 21.8 1.0 N B:THR223 3.9 39.5 1.0 CD2 B:HIS177 4.2 28.3 1.0 NE2 B:HIS173 4.2 28.4 1.0 NE2 B:HIS177 4.2 29.1 1.0 CD2 B:HIS173 4.3 25.4 1.0 N B:CYS222 4.5 38.7 1.0 CA B:THR223 4.5 40.3 1.0 C B:HIS173 4.6 21.2 1.0 O B:HIS173 4.6 21.6 1.0 N B:HIS173 4.6 21.1 1.0 O B:GLN172 4.8 21.9 1.0 CA B:HIS177 4.8 22.8 1.0

B.Calamini, B.D.Santarsiero, J.A.Boutin, A.D.Mesecar. Kinetic, Thermodynamic and X-Ray Structural Insights Into the Interaction of Melatonin and Analogues with Quinone Reductase 2. Biochem.J. V. 413 81 2008.
ISSN: ISSN 0264-6021
PubMed: 18254726
DOI: 10.1042/BJ20071373