Zinc in PDB 3o73: Crystal Structure of Quinone Reductase 2 in Complex with the Indolequinone MAC627

All present enzymatic activity of Crystal Structure of Quinone Reductase 2 in Complex with the Indolequinone MAC627:
1.10.99.2;

The structure of Crystal Structure of Quinone Reductase 2 in Complex with the Indolequinone MAC627, PDB code: 3o73 was solved by M.Dufour, C.Yan, M.A.Colucci, D.Siegel, Y.Li, C.I.De Matteis, D.Ross, C.J.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.45 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.080, 82.050, 106.340, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 28.8

The binding sites of Zinc atom in the Crystal Structure of Quinone Reductase 2 in Complex with the Indolequinone MAC627 (pdb code 3o73). 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 2 in Complex with the Indolequinone MAC627, PDB code: 3o73:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Quinone Reductase 2 in Complex with the Indolequinone MAC627


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 2 in Complex with the Indolequinone MAC627 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn237 b:36.5 occ:1.00 O A:CYS222 2.1 35.4 1.0 ND1 A:HIS173 2.1 30.4 1.0 SG A:CYS222 2.2 30.9 1.0 ND1 A:HIS177 2.2 33.7 1.0 CB A:CYS222 2.8 35.2 1.0 C A:CYS222 2.9 36.0 1.0 CG A:HIS173 3.0 30.0 1.0 CG A:HIS177 3.1 30.6 1.0 CE1 A:HIS173 3.1 35.5 1.0 CE1 A:HIS177 3.2 30.9 1.0 CB A:HIS173 3.2 27.6 1.0 CB A:HIS177 3.4 29.7 1.0 CA A:CYS222 3.4 35.0 1.0 CA A:HIS173 3.6 27.2 1.0 N A:THR223 4.1 36.5 1.0 CD2 A:HIS173 4.1 31.6 1.0 NE2 A:HIS173 4.2 35.5 1.0 NE2 A:HIS177 4.2 31.0 1.0 CD2 A:HIS177 4.2 31.3 1.0 N A:HIS173 4.5 28.1 1.0 N A:CYS222 4.5 36.2 1.0 CA A:THR223 4.6 37.5 1.0 C A:HIS173 4.6 27.6 1.0 O A:HIS173 4.8 25.5 1.0 O A:GLN172 4.8 29.5 1.0 CA A:HIS177 4.9 29.5 1.0 C A:GLN172 4.9 28.4 1.0 CZ3 A:TRP169 5.0 26.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Quinone Reductase 2 in Complex with the Indolequinone MAC627


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 2 in Complex with the Indolequinone MAC627 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn237 b:39.0 occ:1.00 ND1 B:HIS177 1.9 40.5 1.0 SG B:CYS222 2.1 37.3 1.0 ND1 B:HIS173 2.2 33.3 1.0 O B:CYS222 2.2 41.2 1.0 CE1 B:HIS177 2.9 41.8 1.0 CG B:HIS177 2.9 35.8 1.0 CB B:CYS222 3.0 41.3 1.0 C B:CYS222 3.0 40.1 1.0 CG B:HIS173 3.1 28.9 1.0 CE1 B:HIS173 3.2 31.4 1.0 CB B:HIS177 3.3 29.6 1.0 CB B:HIS173 3.3 29.4 1.0 CA B:CYS222 3.5 40.3 1.0 CA B:HIS173 3.5 28.2 1.0 NE2 B:HIS177 4.0 43.6 1.0 CD2 B:HIS177 4.0 37.4 1.0 N B:THR223 4.0 38.8 1.0 CD2 B:HIS173 4.2 31.2 1.0 NE2 B:HIS173 4.2 35.3 1.0 N B:HIS173 4.5 29.3 1.0 C B:HIS173 4.5 28.7 1.0 CA B:THR223 4.6 36.1 1.0 N B:CYS222 4.7 41.4 1.0 O B:HIS173 4.7 29.5 1.0 O B:GLN172 4.8 29.5 1.0 CA B:HIS177 4.8 29.6 1.0 CE1 B:TYR132 4.9 38.8 1.0 CZ3 B:TRP169 4.9 28.0 1.0 C B:GLN172 4.9 28.7 1.0

M.Dufour, C.Yan, D.Siegel, M.A.Colucci, M.Jenner, N.J.Oldham, J.Gomez, P.Reigan, Y.Li, C.I.De Matteis, D.Ross, C.J.Moody. Mechanism-Based Inhibition of Quinone Reductase 2 (NQO2): Selectivity For NQO2 Over NQO1 and Structural Basis For Flavoprotein Inhibition. Chembiochem V. 12 1203 2011.
ISSN: ISSN 1439-4227
PubMed: 21506232
DOI: 10.1002/CBIC.201100085