Chlorine in PDB 5ec8: Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175

All present enzymatic activity of Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175:
2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13;

The structure of Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175, PDB code: 5ec8 was solved by K.Barral, G.Bricogne, A.Sharff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.16 / 1.71
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	61.160, 186.500, 51.610, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 19.7

The binding sites of Chlorine atom in the Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175 (pdb code 5ec8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175, PDB code: 5ec8:

Chlorine binding site 1 out of 1 in the Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Dengue 3 NS5 Methyltransferase Bound to S-Adenosyl Methionine and Compound BF175 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:28.7 occ:0.79 CL A:5LP302 0.0 28.7 0.8 C11 A:5LP302 1.7 24.6 0.8 C10 A:5LP302 2.7 22.3 0.8 C12 A:5LP302 2.7 24.2 0.8 C9 A:5LP302 4.0 26.3 0.8 C13 A:5LP302 4.0 27.2 0.8 CD A:PRO108 4.2 25.1 1.0 CG A:PRO108 4.3 28.5 1.0 C8 A:5LP302 4.5 28.3 0.8 N A:PRO108 4.6 23.5 1.0 CA A:PRO108 4.9 22.4 1.0 CB A:PRO108 4.9 24.0 1.0

F.Benmansour, I.Trist, B.Coutard, E.Decroly, G.Querat, A.Brancale, K.Barral. Discovery of Novel Dengue Virus NS5 Methyltransferase Non-Nucleoside Inhibitors By Fragment-Based Drug Design. Eur.J.Med.Chem. V. 125 865 2016.
ISSN: ISSN 0223-5234
PubMed: 27750202
DOI: 10.1016/J.EJMECH.2016.10.007