Zinc in PDB 3tzb: Quinone Oxidoreductase (NQ02) Bound to NSC13000

All present enzymatic activity of Quinone Oxidoreductase (NQ02) Bound to NSC13000:
1.10.99.2;

The structure of Quinone Oxidoreductase (NQ02) Bound to NSC13000, PDB code: 3tzb was solved by M.S.Dunstan, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.20 / 2.19
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.620, 62.101, 78.506, 92.95, 90.10, 110.45
R / Rfree (%)	16.7 / 23.2

The binding sites of Zinc atom in the Quinone Oxidoreductase (NQ02) Bound to NSC13000 (pdb code 3tzb). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Quinone Oxidoreductase (NQ02) Bound to NSC13000, PDB code: 3tzb:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


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 NSC13000 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn231 b:35.6 occ:1.00 ND1 A:HIS173 2.1 19.7 1.0 ND1 A:HIS177 2.2 33.3 1.0 SG A:CYS222 2.7 51.5 1.0 CB A:CYS222 2.9 87.4 1.0 CE1 A:HIS173 3.0 22.0 1.0 O A:CYS222 3.0 57.5 1.0 CE1 A:HIS177 3.1 30.9 1.0 CG A:HIS177 3.1 38.6 1.0 CG A:HIS173 3.1 16.6 1.0 C A:CYS222 3.3 74.1 1.0 CB A:HIS177 3.4 22.0 1.0 CB A:HIS173 3.5 16.0 1.0 CA A:CYS222 3.6 82.1 1.0 CA A:HIS173 3.8 15.3 1.0 NE2 A:HIS177 4.1 37.3 1.0 N A:THR223 4.1 82.4 1.0 CD2 A:HIS177 4.1 47.1 1.0 NE2 A:HIS173 4.1 29.1 1.0 CD2 A:HIS173 4.2 19.2 1.0 O A:HIS173 4.6 15.7 1.0 C A:HIS173 4.7 13.4 1.0 CA A:THR223 4.8 90.1 1.0 N A:HIS173 4.9 19.4 1.0 CE1 A:TYR132 4.9 15.7 1.0 CD1 A:TYR132 4.9 17.0 1.0 N A:CYS222 4.9 70.2 1.0 CA A:HIS177 5.0 17.1 1.0

Zinc binding site 2 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


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 NSC13000 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn231 b:39.7 occ:1.00 ND1 B:HIS177 2.2 30.4 1.0 ND1 B:HIS173 2.2 29.0 1.0 O B:CYS222 2.6 0.8 1.0 SG B:CYS222 2.8 66.4 1.0 CB B:CYS222 2.9 0.8 1.0 C B:CYS222 3.1 0.4 1.0 CG B:HIS177 3.1 28.1 1.0 CE1 B:HIS173 3.1 32.5 1.0 CE1 B:HIS177 3.2 34.5 1.0 CG B:HIS173 3.3 26.0 1.0 CB B:HIS177 3.4 16.3 1.0 CA B:CYS222 3.6 0.3 1.0 CB B:HIS173 3.6 7.9 1.0 CA B:HIS173 3.8 19.5 1.0 N B:THR223 3.9 0.7 1.0 NE2 B:HIS177 4.2 39.5 1.0 CD2 B:HIS177 4.2 30.8 1.0 NE2 B:HIS173 4.3 32.5 1.0 CD2 B:HIS173 4.4 32.2 1.0 CA B:THR223 4.4 0.7 1.0 N B:CYS222 4.8 94.0 1.0 C B:HIS173 4.8 19.3 1.0 O B:HIS173 4.8 23.0 1.0 N B:HIS173 4.8 22.1 1.0 CA B:HIS177 4.9 14.6 1.0 O B:GLN172 5.0 25.0 1.0

Zinc binding site 3 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Quinone Oxidoreductase (NQ02) Bound to NSC13000 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn231 b:32.2 occ:1.00 ND1 C:HIS173 2.1 19.6 1.0 ND1 C:HIS177 2.4 27.8 1.0 SG C:CYS222 2.5 51.2 1.0 CB C:CYS222 2.8 83.6 1.0 O C:CYS222 2.8 67.8 1.0 CE1 C:HIS173 3.1 20.5 1.0 CG C:HIS173 3.2 19.2 1.0 C C:CYS222 3.3 80.4 1.0 CG C:HIS177 3.3 25.3 1.0 CE1 C:HIS177 3.3 24.0 1.0 CB C:HIS177 3.5 16.5 1.0 CA C:CYS222 3.5 79.4 1.0 CB C:HIS173 3.6 15.6 1.0 CA C:HIS173 3.9 15.5 1.0 NE2 C:HIS173 4.2 26.4 1.0 N C:THR223 4.2 89.1 1.0 CD2 C:HIS173 4.3 17.7 1.0 NE2 C:HIS177 4.4 27.6 1.0 CD2 C:HIS177 4.4 27.0 1.0 O C:HIS173 4.7 22.8 1.0 C C:HIS173 4.7 13.5 1.0 CA C:THR223 4.8 0.3 1.0 N C:CYS222 4.8 61.0 1.0 N C:HIS173 4.9 18.4 1.0 CD1 C:TYR132 5.0 22.6 1.0

Zinc binding site 4 out of 4 in the Quinone Oxidoreductase (NQ02) Bound to NSC13000


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Quinone Oxidoreductase (NQ02) Bound to NSC13000 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn231 b:30.4 occ:1.00 ND1 D:HIS173 2.3 23.1 1.0 ND1 D:HIS177 2.3 28.6 1.0 O D:CYS222 2.6 34.6 1.0 CB D:CYS222 2.7 77.6 1.0 SG D:CYS222 2.7 55.6 1.0 C D:CYS222 3.1 63.5 1.0 CG D:HIS177 3.2 26.9 1.0 CE1 D:HIS173 3.2 19.1 1.0 CE1 D:HIS177 3.2 24.0 1.0 CG D:HIS173 3.2 25.8 1.0 CA D:CYS222 3.4 71.8 1.0 CB D:HIS177 3.5 16.5 1.0 CB D:HIS173 3.5 14.2 1.0 CA D:HIS173 3.7 14.4 1.0 N D:THR223 4.1 79.6 1.0 NE2 D:HIS177 4.3 27.2 1.0 CD2 D:HIS177 4.3 27.9 1.0 NE2 D:HIS173 4.3 28.3 1.0 CD2 D:HIS173 4.4 27.7 1.0 C D:HIS173 4.7 9.7 1.0 N D:HIS173 4.7 12.4 1.0 N D:CYS222 4.7 63.7 1.0 CA D:THR223 4.8 93.2 1.0 O D:HIS173 4.8 21.0 1.0 O D:GLN172 5.0 24.4 1.0

K.A.Nolan, M.S.Dunstan, M.C.Caraher, K.A.Scott, D.Leys, I.J.Stratford. In Silico Screening Reveals Structurally Diverse, Nanomolar Inhibitors of NQO2 That Are Functionally Active in Cells and Can Modulate Nf-Kappa B Signaling. Mol.Cancer Ther. V. 11 194 2012.
ISSN: ISSN 1535-7163
PubMed: 22090421
DOI: 10.1158/1535-7163.MCT-11-0543