Zinc in PDB 4qoe: The Value 'Crystal Structure of Fad Quinone Reductase 2 at 1.45A

All present enzymatic activity of The Value 'Crystal Structure of Fad Quinone Reductase 2 at 1.45A:
1.10.99.2;

The structure of The Value 'Crystal Structure of Fad Quinone Reductase 2 at 1.45A, PDB code: 4qoe 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)	44.97 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.410, 83.190, 106.900, 90.00, 90.00, 90.00
R / Rfree (%)	12.6 / 16

The binding sites of Zinc atom in the The Value 'Crystal Structure of Fad Quinone Reductase 2 at 1.45A (pdb code 4qoe). 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 Fad Quinone Reductase 2 at 1.45A, PDB code: 4qoe:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Value 'Crystal Structure of Fad Quinone Reductase 2 at 1.45A


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 Fad Quinone Reductase 2 at 1.45A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:17.3 occ:1.00 O A:CYS222 2.0 18.1 1.0 ND1 A:HIS173 2.1 17.4 1.0 ND1 A:HIS177 2.1 16.8 1.0 SG A:CYS222 2.2 17.3 1.0 CB A:CYS222 2.9 17.1 1.0 C A:CYS222 2.9 17.4 1.0 CE1 A:HIS173 3.0 16.9 1.0 CG A:HIS173 3.1 16.5 1.0 CE1 A:HIS177 3.1 18.5 1.0 CG A:HIS177 3.1 15.1 1.0 CB A:HIS177 3.3 13.6 1.0 CB A:HIS173 3.4 13.9 1.0 CA A:CYS222 3.4 16.3 1.0 CA A:HIS173 3.6 13.0 1.0 N A:THR223 4.0 18.4 1.0 NE2 A:HIS173 4.1 17.3 1.0 CD2 A:HIS173 4.2 15.7 1.0 NE2 A:HIS177 4.2 20.0 1.0 CD2 A:HIS177 4.2 17.4 1.0 N A:HIS173 4.5 14.6 1.0 CA A:THR223 4.6 18.4 1.0 N A:CYS222 4.6 18.7 1.0 O A:GLN172 4.6 13.9 1.0 C A:HIS173 4.6 15.1 1.0 O A:HIS173 4.6 14.5 1.0 CA A:HIS177 4.8 12.8 1.0 C A:GLN172 4.9 13.3 1.0 CZ3 A:TRP169 5.0 18.6 1.0

Zinc binding site 2 out of 2 in the The Value 'Crystal Structure of Fad Quinone Reductase 2 at 1.45A


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 Fad Quinone Reductase 2 at 1.45A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:31.9 occ:1.00 ND1 B:HIS173 2.0 27.8 1.0 O B:CYS222 2.0 27.6 1.0 ND1 B:HIS177 2.1 33.9 1.0 SG B:CYS222 2.3 28.5 1.0 C B:CYS222 2.9 26.2 1.0 CB B:CYS222 2.9 27.0 1.0 CE1 B:HIS173 2.9 30.9 1.0 CG B:HIS177 3.0 29.8 1.0 CG B:HIS173 3.1 26.1 1.0 CE1 B:HIS177 3.2 42.5 1.0 CB B:HIS177 3.2 25.2 1.0 CA B:CYS222 3.4 32.4 1.0 CB B:HIS173 3.5 18.8 1.0 CA B:HIS173 3.7 18.9 1.0 N B:THR223 4.0 34.6 1.0 NE2 B:HIS173 4.1 28.6 1.0 CD2 B:HIS173 4.1 24.6 1.0 CD2 B:HIS177 4.2 32.2 1.0 NE2 B:HIS177 4.2 39.1 1.0 N B:CYS222 4.6 35.4 1.0 N B:HIS173 4.6 20.8 1.0 O B:GLN172 4.6 20.8 1.0 O B:HIS173 4.6 23.3 1.0 C B:HIS173 4.6 16.3 1.0 CA B:THR223 4.6 36.9 1.0 CA B:HIS177 4.7 20.9 1.0 CD1 B:TYR132 4.8 17.4 0.5 CE1 B:TYR132 4.9 15.8 0.5 C B:GLN172 4.9 17.8 1.0 CE1 B:TYR132 4.9 17.0 0.5 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 Fad Quinone Reductase 2 at 1.45A To Be Published.