Zinc in PDB 3fw1: Quinone Reductase 2

All present enzymatic activity of Quinone Reductase 2:
1.10.99.2;

The structure of Quinone Reductase 2, PDB code: 3fw1 was solved by J.A.Winger, O.Hantschel, G.Superti-Furga, J.Kuriyan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.86 / 1.75
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	100.337, 100.337, 104.858, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 18.2

The binding sites of Zinc atom in the Quinone Reductase 2 (pdb code 3fw1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Quinone Reductase 2, PDB code: 3fw1:

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Quinone Reductase 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn231 b:23.9 occ:0.65 HB3 A:CYS222 1.7 41.3 0.5 O A:CYS222 2.2 36.0 0.5 SG A:CYS222 2.2 15.0 0.5 ND1 A:HIS177 2.2 27.1 1.0 O A:CYS222 2.2 36.3 0.5 ND1 A:HIS173 2.3 25.7 1.0 HB3 A:CYS222 2.5 37.5 0.5 CB A:CYS222 2.7 34.7 0.5 HA A:HIS173 2.7 17.7 1.0 CB A:CYS222 2.8 31.5 0.5 C A:CYS222 2.9 36.8 0.5 C A:CYS222 2.9 38.1 0.5 HB3 A:HIS177 3.0 19.4 1.0 CG A:HIS177 3.0 24.5 1.0 HB2 A:HIS173 3.1 21.0 1.0 HB2 A:HIS177 3.1 19.4 1.0 CG A:HIS173 3.2 20.7 1.0 HB2 A:CYS222 3.2 41.3 0.5 CB A:HIS177 3.2 16.5 1.0 CE1 A:HIS177 3.3 31.4 1.0 CE1 A:HIS173 3.3 29.3 1.0 CA A:CYS222 3.3 31.4 0.5 CB A:HIS173 3.4 17.7 1.0 CA A:CYS222 3.4 29.4 0.5 CA A:HIS173 3.5 15.0 1.0 HE1 A:HIS177 3.5 37.4 1.0 HE1 A:HIS173 3.5 34.8 1.0 SG A:CYS222 3.6 29.2 0.5 HB2 A:CYS222 3.6 37.5 0.5 HA A:CYS222 3.8 37.4 0.5 HA A:CYS222 3.9 34.9 0.5 N A:THR223 4.0 32.9 1.0 HA A:THR223 4.0 28.5 1.0 CD2 A:HIS177 4.2 28.2 1.0 HE1 A:HIS227 4.3 30.5 1.0 NE2 A:HIS177 4.3 25.6 1.0 CD2 A:HIS173 4.3 19.2 1.0 HB3 A:HIS173 4.3 21.0 1.0 NE2 A:HIS173 4.4 21.5 1.0 O A:GLN172 4.4 17.1 1.0 N A:HIS173 4.4 15.2 1.0 C A:HIS173 4.5 15.1 1.0 O A:HIS173 4.5 16.3 1.0 CA A:THR223 4.5 24.0 1.0 N A:CYS222 4.6 32.2 0.5 N A:CYS222 4.6 32.1 0.5 H A:CYS222 4.6 38.3 0.5 HE1 A:TYR132 4.6 20.4 1.0 H A:CYS222 4.6 38.3 0.5 H A:THR223 4.7 39.1 1.0 HD1 A:TYR132 4.7 19.1 1.0 HZ3 A:TRP169 4.7 32.8 1.0 C A:GLN172 4.7 21.5 1.0 CA A:HIS177 4.8 16.0 1.0 O A:HOH398 4.9 46.2 1.0 H A:HIS173 5.0 17.9 1.0

J.A.Winger, O.Hantschel, G.Superti-Furga, J.Kuriyan. The Structure of the Leukemia Drug Imatinib Bound to Human Quinone Reductase 2 (NQO2). Bmc Struct.Biol. V. 9 7 2009.
ISSN: ESSN 1472-6807
PubMed: 19236722
DOI: 10.1186/1472-6807-9-7