Zinc in PDB 2qr2: Human Quinone Reductase Type 2, Complex with Menadione

All present enzymatic activity of Human Quinone Reductase Type 2, Complex with Menadione:
1.6.99.2;

The structure of Human Quinone Reductase Type 2, Complex with Menadione, PDB code: 2qr2 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 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.600, 106.270, 56.080, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 27.4

The binding sites of Zinc atom in the Human Quinone Reductase Type 2, Complex with Menadione (pdb code 2qr2). 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, Complex with Menadione, PDB code: 2qr2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Quinone Reductase Type 2, Complex with Menadione


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, Complex with Menadione within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn231 b:56.9 occ:1.00 ND1 A:HIS177 1.9 43.6 1.0 SG A:CYS222 2.4 53.6 1.0 ND1 A:HIS173 2.5 45.1 1.0 O A:CYS222 2.6 55.4 1.0 CB A:CYS222 2.6 54.3 1.0 CG A:HIS177 2.7 38.2 1.0 CB A:HIS177 2.9 33.1 1.0 CE1 A:HIS177 3.0 42.5 1.0 CG A:HIS173 3.3 41.4 1.0 C A:CYS222 3.3 55.4 1.0 CE1 A:HIS173 3.4 44.5 1.0 CA A:CYS222 3.5 54.3 1.0 CB A:HIS173 3.5 36.7 1.0 CA A:HIS173 3.5 31.6 1.0 CD2 A:HIS177 3.8 40.3 1.0 NE2 A:HIS177 4.0 42.9 1.0 O A:GLN172 4.2 30.4 1.0 N A:HIS173 4.4 30.2 1.0 CA A:HIS177 4.4 29.0 1.0 CD2 A:HIS173 4.4 43.1 1.0 NE2 A:HIS173 4.5 43.6 1.0 N A:THR223 4.5 55.8 1.0 O A:HIS173 4.5 32.2 1.0 C A:HIS173 4.5 31.1 1.0 C A:GLN172 4.7 27.4 1.0 N A:CYS222 4.7 53.0 1.0 H A:HIS177 4.8 0.0 0.0 H A:CYS222 4.9 0.0 0.0 HE2 A:HIS177 4.9 0.0 0.0

Zinc binding site 2 out of 2 in the Human Quinone Reductase Type 2, Complex with Menadione


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, Complex with Menadione within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn232 b:52.3 occ:1.00 SG B:CYS222 2.3 45.9 1.0 ND1 B:HIS173 2.3 41.5 1.0 ND1 B:HIS177 2.4 35.8 1.0 O B:CYS222 2.5 51.0 1.0 CB B:CYS222 2.8 48.2 1.0 CG B:HIS173 3.1 38.6 1.0 CG B:HIS177 3.2 28.6 1.0 C B:CYS222 3.2 50.3 1.0 CE1 B:HIS173 3.3 41.6 1.0 CB B:HIS177 3.3 24.6 1.0 CB B:HIS173 3.4 34.1 1.0 CE1 B:HIS177 3.4 33.0 1.0 CA B:HIS173 3.5 30.6 1.0 CA B:CYS222 3.5 49.3 1.0 CD2 B:HIS173 4.3 40.6 1.0 N B:THR223 4.3 50.5 1.0 NE2 B:HIS173 4.3 41.7 1.0 CD2 B:HIS177 4.4 31.2 1.0 N B:HIS173 4.4 28.2 1.0 O B:HIS173 4.4 30.5 1.0 O B:GLN172 4.4 29.8 1.0 C B:HIS173 4.4 30.6 1.0 NE2 B:HIS177 4.5 32.3 1.0 C B:GLN172 4.8 27.1 1.0 N B:CYS222 4.8 47.6 1.0 CA B:HIS177 4.9 22.4 1.0 CA B:THR223 4.9 50.2 1.0 H B:THR223 5.0 0.0 0.0

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