Fluorine in PDB 6uy4: Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni

All present enzymatic activity of Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni:
1.3.98.1;

The structure of Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni, PDB code: 6uy4 was solved by R.M.Mori, L.C.C.Zapata, M.C.Nonato, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.00 / 2.80
Space group	I 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	187.981, 187.981, 187.981, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 24.6

The binding sites of Fluorine atom in the Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni (pdb code 6uy4). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni, PDB code: 6uy4:

Fluorine binding site 1 out of 1 in the Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Dihydroorotate Dehydrogenase From Schistosoma Mansoni within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:0.3 occ:1.00 F1 A:QLA401 0.0 0.3 1.0 C7 A:QLA401 1.4 0.0 1.0 C6 A:QLA401 2.3 0.6 1.0 C8 A:QLA401 2.3 0.9 1.0 CD A:PRO362 3.2 85.2 1.0 C5 A:QLA401 3.6 0.8 1.0 C9 A:QLA401 3.6 0.9 1.0 CG A:PRO362 3.8 80.8 1.0 CA A:GLY361 4.0 86.4 1.0 N A:PRO362 4.1 85.8 1.0 C4 A:QLA401 4.1 0.6 1.0 CZ A:PHE357 4.2 86.3 1.0 CE1 A:PHE357 4.4 88.4 1.0 C A:GLY361 4.4 85.8 1.0 CD2 A:LEU36 4.6 92.0 1.0 O A:PHE357 4.9 92.5 1.0 CE2 A:PHE357 4.9 83.4 1.0

R.M.Mori, M.A.A.Aleixo, L.C.C.Zapata, F.A.Calil, F.D.S.Emery, M.C.Nonato. Structural Basis For the Function and Inhibition of Dihydroorotate Dehydrogenase From Schistosoma Mansoni. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 32428996
DOI: 10.1111/FEBS.15367