Zinc in PDB 4qod: The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A

All present enzymatic activity of The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A:
1.10.99.2;

The structure of The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A, PDB code: 4qod was solved by J.Serriere, J.A.Boutin, T.Isabet, M.Antoine, G.Ferry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.65 / 1.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.120, 83.200, 106.540, 90.00, 90.00, 90.00
R / Rfree (%)	15.1 / 19.1

The binding sites of Zinc atom in the The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A (pdb code 4qod). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A, PDB code: 4qod:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn305 b:17.0 occ:1.00 O A:CYS222 2.0 17.9 1.0 ND1 A:HIS177 2.1 17.1 1.0 ND1 A:HIS173 2.1 15.7 1.0 SG A:CYS222 2.2 17.5 1.0 CB A:CYS222 2.8 18.4 1.0 C A:CYS222 2.9 17.5 1.0 CE1 A:HIS173 3.0 18.5 1.0 CE1 A:HIS177 3.0 17.4 1.0 CG A:HIS177 3.0 15.7 1.0 CG A:HIS173 3.1 15.7 1.0 CB A:HIS177 3.3 14.2 1.0 CA A:CYS222 3.4 17.6 1.0 CB A:HIS173 3.5 14.4 1.0 CA A:HIS173 3.6 12.1 1.0 N A:THR223 4.0 18.6 1.0 NE2 A:HIS177 4.1 17.4 1.0 NE2 A:HIS173 4.1 18.6 1.0 CD2 A:HIS177 4.2 15.8 1.0 CD2 A:HIS173 4.2 15.9 1.0 N A:HIS173 4.5 12.1 1.0 N A:CYS222 4.5 20.0 1.0 CA A:THR223 4.6 18.6 1.0 C A:HIS173 4.7 15.2 1.0 O A:GLN172 4.7 13.9 1.0 O A:HIS173 4.7 15.2 1.0 CA A:HIS177 4.8 14.0 1.0 C A:GLN172 4.9 12.7 1.0 CZ3 A:TRP169 5.0 17.2 1.0

Zinc binding site 2 out of 2 in the The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn303 b:27.3 occ:1.00 O B:CYS222 1.8 25.3 1.0 ND1 B:HIS173 2.1 23.4 1.0 SG B:CYS222 2.2 26.3 1.0 ND1 B:HIS177 2.2 33.5 1.0 C B:CYS222 2.5 23.1 1.0 CB B:CYS222 2.7 34.2 1.0 CE1 B:HIS173 3.0 29.2 1.0 CG B:HIS177 3.0 28.6 1.0 CG B:HIS173 3.1 24.9 1.0 CA B:CYS222 3.1 32.2 1.0 CB B:HIS177 3.2 24.7 1.0 CE1 B:HIS177 3.3 32.9 1.0 CB B:HIS173 3.5 20.9 1.0 N B:THR223 3.7 29.6 1.0 CA B:HIS173 3.7 20.2 1.0 NE2 B:HIS173 4.1 26.4 1.0 CD2 B:HIS173 4.2 25.3 1.0 CD2 B:HIS177 4.2 26.1 1.0 NE2 B:HIS177 4.3 33.5 1.0 N B:CYS222 4.3 33.0 1.0 CA B:THR223 4.4 33.7 1.0 N B:HIS173 4.6 21.9 1.0 CD1 B:TYR132 4.7 17.8 0.5 C B:HIS173 4.7 18.1 1.0 CE1 B:TYR132 4.7 14.2 0.5 O B:GLN172 4.7 21.2 1.0 CA B:HIS177 4.8 21.8 1.0 O B:HIS173 4.8 22.9 1.0 CE1 B:HIS227 4.9 25.9 1.0 CE1 B:TYR132 4.9 23.9 0.5 C B:GLN172 5.0 19.0 1.0 CZ3 B:TRP169 5.0 25.0 1.0

J.Serriere, J.A.Boutin, T.Isabet, M.Antoine, G.Ferry. The Value Crystal Structure of Apo Quinone Reductase 2 at 1.35A To Be Published.