Zinc in PDB 3te7: Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1

All present enzymatic activity of Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1:
1.10.99.2;

The structure of Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1, PDB code: 3te7 was solved by M.S.Dunstan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.89 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.910, 84.030, 106.550, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20.6

The binding sites of Zinc atom in the Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1 (pdb code 3te7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1, PDB code: 3te7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn231 b:20.1 occ:1.00 ND1 A:HIS173 2.1 18.6 1.0 ND1 A:HIS177 2.1 22.6 1.0 O A:CYS222 2.2 20.5 1.0 SG A:CYS222 2.2 16.9 1.0 CB A:CYS222 2.8 17.2 1.0 C A:CYS222 3.0 23.4 1.0 CE1 A:HIS173 3.0 21.2 1.0 CG A:HIS177 3.0 17.2 1.0 CG A:HIS173 3.1 14.7 1.0 CE1 A:HIS177 3.2 25.4 1.0 CB A:HIS177 3.3 10.5 1.0 CA A:CYS222 3.4 16.9 1.0 CB A:HIS173 3.5 16.5 1.0 CA A:HIS173 3.6 16.9 1.0 N A:THR223 4.1 20.1 1.0 NE2 A:HIS173 4.2 17.9 1.0 CD2 A:HIS177 4.2 21.9 1.0 CD2 A:HIS173 4.2 16.7 1.0 NE2 A:HIS177 4.2 24.2 1.0 N A:HIS173 4.5 16.0 1.0 O A:GLN172 4.6 13.0 1.0 N A:CYS222 4.6 19.7 1.0 C A:HIS173 4.6 16.7 1.0 CA A:THR223 4.6 21.1 1.0 O A:HIS173 4.6 13.5 1.0 CA A:HIS177 4.8 12.8 1.0 C A:GLN172 4.9 12.6 1.0

Zinc binding site 2 out of 2 in the Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Quinone Oxidoreductase (NQ02) Bound to the Imidazoacridin-6-One 5A1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn231 b:27.1 occ:1.00 ND1 B:HIS173 2.0 25.6 1.0 ND1 B:HIS177 2.1 26.3 1.0 O B:CYS222 2.2 25.1 1.0 SG B:CYS222 2.3 25.6 1.0 CB B:CYS222 2.8 24.8 1.0 C B:CYS222 3.0 33.8 1.0 CG B:HIS177 3.0 22.8 1.0 CG B:HIS173 3.0 22.4 1.0 CE1 B:HIS173 3.0 29.1 1.0 CE1 B:HIS177 3.2 26.9 1.0 CB B:HIS177 3.2 20.2 1.0 CB B:HIS173 3.3 20.1 1.0 CA B:CYS222 3.5 31.2 1.0 CA B:HIS173 3.6 20.2 1.0 N B:THR223 4.1 33.6 1.0 NE2 B:HIS173 4.1 23.4 1.0 CD2 B:HIS173 4.1 18.1 1.0 CD2 B:HIS177 4.2 25.1 1.0 NE2 B:HIS177 4.2 27.5 1.0 O B:HOH453 4.3 49.7 1.0 N B:HIS173 4.6 20.6 1.0 C B:HIS173 4.6 19.6 1.0 CA B:THR223 4.6 29.8 1.0 N B:CYS222 4.6 32.2 1.0 O B:HIS173 4.6 20.7 1.0 O B:GLN172 4.7 20.7 1.0 CA B:HIS177 4.7 22.2 1.0 C B:GLN172 5.0 22.5 1.0 CE1 B:TYR132 5.0 22.2 1.0 CD1 B:TYR132 5.0 23.6 1.0

M.S.Dunstan, J.Barnes, M.Humphries, R.C.Whitehead, R.A.Bryce, D.Leys, I.J.Stratford, K.A.Nolan. Novel Inhibitors of Nrh:Quinone Oxidoreductase 2 (NQO2): Crystal Structures, Biochemical Activity, and Intracellular Effects of Imidazoacridin-6-Ones. J.Med.Chem. V. 54 6597 2011.
ISSN: ISSN 0022-2623
PubMed: 21859103
DOI: 10.1021/JM200416E