Zinc in PDB 4qof: Crystal Structure of Fmn Quinone Reductase 2 at 1.55A

All present enzymatic activity of Crystal Structure of Fmn Quinone Reductase 2 at 1.55A:
1.10.99.2;

The structure of Crystal Structure of Fmn Quinone Reductase 2 at 1.55A, PDB code: 4qof 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)	22.69 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.170, 83.270, 106.440, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 23.5

The binding sites of Zinc atom in the Crystal Structure of Fmn Quinone Reductase 2 at 1.55A (pdb code 4qof). 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 Fmn Quinone Reductase 2 at 1.55A, PDB code: 4qof:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Fmn Quinone Reductase 2 at 1.55A


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 Fmn Quinone Reductase 2 at 1.55A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:17.4 occ:1.00 ND1 A:HIS173 2.0 17.9 1.0 ND1 A:HIS177 2.0 17.6 1.0 O A:CYS222 2.1 14.7 1.0 SG A:CYS222 2.4 19.6 1.0 CB A:CYS222 2.8 16.5 1.0 C A:CYS222 2.9 18.5 1.0 CE1 A:HIS173 3.0 17.8 1.0 CG A:HIS177 3.0 15.5 1.0 CG A:HIS173 3.0 15.9 1.0 CE1 A:HIS177 3.1 18.1 1.0 CB A:HIS177 3.3 12.7 1.0 CB A:HIS173 3.4 13.5 1.0 CA A:CYS222 3.4 17.1 1.0 CA A:HIS173 3.6 12.4 1.0 N A:THR223 4.0 16.8 1.0 NE2 A:HIS173 4.2 17.8 1.0 CD2 A:HIS173 4.2 17.3 1.0 CD2 A:HIS177 4.2 17.5 1.0 NE2 A:HIS177 4.2 18.3 1.0 N A:HIS173 4.5 11.8 1.0 CA A:THR223 4.6 18.1 1.0 N A:CYS222 4.6 18.0 1.0 C A:HIS173 4.6 14.7 1.0 O A:HIS173 4.6 14.9 1.0 O A:GLN172 4.7 13.2 1.0 CA A:HIS177 4.8 11.7 1.0 C A:GLN172 4.9 13.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Fmn Quinone Reductase 2 at 1.55A


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 Fmn Quinone Reductase 2 at 1.55A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:24.6 occ:1.00 O B:CYS222 2.0 27.3 1.0 ND1 B:HIS173 2.1 31.9 1.0 ND1 B:HIS177 2.1 34.9 1.0 SG B:CYS222 2.3 29.6 1.0 CB B:CYS222 2.7 27.6 1.0 C B:CYS222 2.8 31.1 1.0 CE1 B:HIS173 3.1 32.4 1.0 CG B:HIS177 3.1 31.0 1.0 CG B:HIS173 3.1 28.7 1.0 CE1 B:HIS177 3.1 35.3 1.0 CA B:CYS222 3.3 27.9 1.0 CB B:HIS177 3.4 25.1 1.0 CB B:HIS173 3.4 24.4 1.0 CA B:HIS173 3.7 22.9 1.0 N B:THR223 3.9 32.4 1.0 NE2 B:HIS173 4.2 31.9 1.0 CD2 B:HIS173 4.2 30.2 1.0 CD2 B:HIS177 4.3 34.3 1.0 NE2 B:HIS177 4.3 35.9 1.0 N B:CYS222 4.5 29.9 1.0 CA B:THR223 4.5 33.2 1.0 N B:HIS173 4.6 22.8 1.0 C B:HIS173 4.7 23.3 1.0 O B:HIS173 4.7 23.8 1.0 O B:GLN172 4.7 26.0 1.0 CA B:HIS177 4.9 23.1 1.0 CE1 B:HIS227 4.9 30.3 1.0 C B:GLN172 5.0 24.7 1.0

J.Serriere, J.A.Boutin, T.Isabet, M.Antoine, G.Ferry. Crystal Structure of Fmn Quinone Reductase 2 at 1.55A To Be Published.