Fluorine in PDB 8pts: Human GUK1 in Complex with Compound AT8001

All present enzymatic activity of Human GUK1 in Complex with Compound AT8001:
2.7.4.8;

The structure of Human GUK1 in Complex with Compound AT8001, PDB code: 8pts was solved by C.Zimberger, B.Canard, F.Ferron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.85 / 1.76
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.773, 54.273, 58.957, 90, 108.79, 90
R / Rfree (%)	24.8 / 26

The binding sites of Fluorine atom in the Human GUK1 in Complex with Compound AT8001 (pdb code 8pts). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human GUK1 in Complex with Compound AT8001, PDB code: 8pts:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human GUK1 in Complex with Compound AT8001


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human GUK1 in Complex with Compound AT8001 within 5.0Å range: probe atom residue distance (Å) B Occ A:F201 b:42.8 occ:1.00 F A:EIF201 0.0 42.8 1.0 C1 A:EIF201 1.4 42.3 1.0 C A:EIF201 2.3 43.1 1.0 C5 A:EIF201 2.4 41.1 1.0 C2 A:EIF201 2.4 41.9 1.0 H6 A:EIF201 2.5 42.5 0.0 H2 A:EIF201 2.5 41.1 0.0 H4 A:EIF201 2.6 43.1 0.0 H5 A:EIF201 2.7 43.1 0.0 O A:EIF201 2.7 42.5 1.0 H1 A:EIF201 2.8 41.2 0.0 C3 A:EIF201 3.0 41.2 1.0 O5 A:EIF201 3.2 40.9 1.0 H3 A:EIF201 3.3 43.1 0.0 H A:EIF201 3.3 41.9 0.0 N A:EIF201 3.6 39.7 1.0 CD2 A:PHE76 4.1 53.6 1.0 CE2 A:PHE76 4.3 54.8 1.0 C8 A:EIF201 4.3 39.1 1.0 N2 A:EIF201 4.3 38.7 1.0 C4 A:EIF201 4.5 40.6 1.0 O A:HOH346 4.5 56.7 1.0 C6 A:EIF201 4.6 39.0 1.0 CG A:PHE76 4.7 52.2 1.0 H7 A:EIF201 4.8 40.6 0.0 H11 A:EIF201 4.8 39.0 0.0 CZ A:PHE76 5.0 54.7 1.0

Fluorine binding site 2 out of 2 in the Human GUK1 in Complex with Compound AT8001


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human GUK1 in Complex with Compound AT8001 within 5.0Å range: probe atom residue distance (Å) B Occ B:F201 b:32.8 occ:1.00 F B:EIF201 0.0 32.8 1.0 C1 B:EIF201 1.4 31.7 1.0 C B:EIF201 2.3 30.9 1.0 C5 B:EIF201 2.4 30.3 1.0 H2 B:EIF201 2.4 30.3 0.0 C2 B:EIF201 2.4 32.4 1.0 H5 B:EIF201 2.5 30.9 0.0 H1 B:EIF201 2.6 31.3 0.0 O B:EIF201 2.7 33.8 1.0 H3 B:EIF201 2.7 30.9 0.0 C3 B:EIF201 2.9 31.3 1.0 O5 B:EIF201 3.2 31.0 1.0 H6 B:EIF201 3.3 33.8 0.0 H4 B:EIF201 3.3 30.9 0.0 H B:EIF201 3.4 32.4 0.0 N B:EIF201 3.6 28.8 1.0 CD2 B:PHE76 4.1 40.1 1.0 N2 B:EIF201 4.2 27.0 1.0 CE2 B:PHE76 4.3 40.8 1.0 C8 B:EIF201 4.3 27.8 1.0 C4 B:EIF201 4.3 30.9 1.0 C6 B:EIF201 4.6 27.8 1.0 CG B:PHE76 4.6 38.1 1.0 H7 B:EIF201 4.6 30.9 0.0 H11 B:EIF201 4.8 27.8 0.0 H8 B:EIF201 4.9 30.9 0.0 CZ B:PHE76 5.0 40.6 1.0

A.Chazot, C.Zimberger, M.Feracci, A.Moussa, S.Good, J.P.Sommadossi, K.Alvarez, F.Ferron, B.Canard. Structural and Functional Basis For Metabolic Activation of the Antiviral Drug Bemnifosbuvir To Be Published.