Zinc in PDB 1qr2: Human Quinone Reductase Type 2

All present enzymatic activity of Human Quinone Reductase Type 2:
1.6.99.2;

The structure of Human Quinone Reductase Type 2, PDB code: 1qr2 was solved by C.Foster, M.A.Bianchet, P.Talalay, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.157, 106.231, 56.615, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 28.4

The binding sites of Zinc atom in the Human Quinone Reductase Type 2 (pdb code 1qr2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Quinone Reductase Type 2, PDB code: 1qr2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Quinone Reductase Type 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Quinone Reductase Type 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn231 b:29.4 occ:1.00 ND1 A:HIS177 1.9 22.5 1.0 SG A:CYS222 2.1 23.8 1.0 ND1 A:HIS173 2.2 24.4 1.0 O A:CYS222 2.2 25.4 1.0 CB A:CYS222 2.7 25.1 1.0 CG A:HIS177 2.9 22.3 1.0 CE1 A:HIS177 3.0 21.9 1.0 C A:CYS222 3.0 25.0 1.0 CE1 A:HIS173 3.1 21.5 1.0 CG A:HIS173 3.2 21.3 1.0 CB A:HIS177 3.2 21.7 1.0 CA A:CYS222 3.4 24.7 1.0 CB A:HIS173 3.5 17.8 1.0 CA A:HIS173 3.7 18.9 1.0 H1 A:HOH261 3.9 0.0 0.0 CD2 A:HIS177 4.1 23.1 1.0 NE2 A:HIS177 4.1 21.3 1.0 N A:THR223 4.1 24.0 1.0 NE2 A:HIS173 4.2 24.0 1.0 CD2 A:HIS173 4.3 23.6 1.0 N A:HIS173 4.6 19.7 1.0 O A:HOH261 4.6 29.8 1.0 N A:CYS222 4.6 25.1 1.0 O A:HIS173 4.6 20.1 1.0 C A:HIS173 4.6 18.5 1.0 O A:GLN172 4.6 18.0 1.0 CA A:THR223 4.7 23.4 1.0 CA A:HIS177 4.7 19.8 1.0 H A:CYS222 4.8 0.0 0.0 H A:THR223 4.9 0.0 0.0 C A:GLN172 4.9 17.9 1.0 CE1 A:TYR132 5.0 31.8 1.0 HE2 A:HIS177 5.0 0.0 0.0

Zinc binding site 2 out of 2 in the Human Quinone Reductase Type 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Quinone Reductase Type 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn232 b:23.6 occ:1.00 ND1 B:HIS177 2.1 18.3 1.0 O B:CYS222 2.2 20.6 1.0 ND1 B:HIS173 2.3 23.6 1.0 SG B:CYS222 2.3 17.2 1.0 CB B:CYS222 2.7 20.6 1.0 C B:CYS222 3.0 20.8 1.0 CG B:HIS177 3.0 16.5 1.0 CE1 B:HIS177 3.2 16.7 1.0 CG B:HIS173 3.2 19.8 1.0 CE1 B:HIS173 3.3 23.5 1.0 CB B:HIS177 3.3 15.8 1.0 CA B:CYS222 3.4 21.1 1.0 CB B:HIS173 3.4 18.6 1.0 CA B:HIS173 3.6 18.9 1.0 H2 B:HOH270 4.0 0.0 0.0 N B:THR223 4.1 20.1 1.0 CD2 B:HIS177 4.2 16.2 1.0 NE2 B:HIS177 4.3 13.3 1.0 CD2 B:HIS173 4.3 21.3 1.0 NE2 B:HIS173 4.4 24.3 1.0 N B:HIS173 4.6 18.5 1.0 N B:CYS222 4.6 18.9 1.0 C B:HIS173 4.6 19.2 1.0 O B:HIS173 4.7 18.4 1.0 CA B:THR223 4.7 18.6 1.0 O B:GLN172 4.8 21.6 1.0 CA B:HIS177 4.8 15.5 1.0 H B:CYS222 4.8 0.0 0.0 O B:HOH270 4.8 25.7 1.0 H B:THR223 4.8 0.0 0.0 O B:HOH284 5.0 27.4 1.0 C B:GLN172 5.0 18.1 1.0

C.E.Foster, M.A.Bianchet, P.Talalay, Q.Zhao, L.M.Amzel. Crystal Structure of Human Quinone Reductase Type 2, A Metalloflavoprotein. Biochemistry V. 38 9881 1999.
ISSN: ISSN 0006-2960
PubMed: 10433694
DOI: 10.1021/BI990799V