Fluorine in PDB 8f99: Compound 10 Bound to Procaspase-6

All present enzymatic activity of Compound 10 Bound to Procaspase-6:
3.4.22.59;

The structure of Compound 10 Bound to Procaspase-6, PDB code: 8f99 was solved by P.Fan, Y.Zhao, A.R.Renslo, M.R.Arkin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.90 / 2.86
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	101.481, 101.481, 321.539, 90, 90, 120
R / Rfree (%)	20 / 24.6

The binding sites of Fluorine atom in the Compound 10 Bound to Procaspase-6 (pdb code 8f99). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Compound 10 Bound to Procaspase-6, PDB code: 8f99:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Compound 10 Bound to Procaspase-6


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Compound 10 Bound to Procaspase-6 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:42.6 occ:0.50 F A:XMR301 0.0 42.6 0.5 C1 A:XMR301 1.3 41.8 0.5 C2 A:XMR301 2.4 40.3 0.5 C6 A:XMR301 2.4 40.8 0.5 N B:SER196 3.4 62.6 1.0 C B:SER196 3.5 61.3 1.0 C B:ALA195 3.6 57.2 1.0 CA B:SER196 3.6 61.5 1.0 C3 A:XMR301 3.6 40.5 0.5 C5 A:XMR301 3.6 42.5 0.5 O B:ALA195 3.7 58.9 1.0 O B:SER196 3.7 63.2 1.0 CA B:GLU214 3.7 72.5 1.0 N B:VAL197 3.8 57.2 1.0 O B:VAL197 3.9 64.0 1.0 CB B:ALA195 3.9 59.8 1.0 N B:GLU214 4.1 68.6 1.0 C4 A:XMR301 4.1 44.4 0.5 C B:VAL197 4.2 59.1 1.0 CB B:GLU214 4.2 77.6 1.0 CA B:ALA195 4.3 57.3 1.0 CG B:GLU214 4.5 84.6 1.0 N B:TYR198 4.7 56.6 1.0 CA B:VAL197 4.7 56.0 1.0 C B:ALA213 4.7 62.2 1.0 O1 A:XMR301 4.7 36.7 0.5 O B:ALA213 4.9 56.0 1.0 C B:GLU214 4.9 68.6 1.0

Fluorine binding site 2 out of 4 in the Compound 10 Bound to Procaspase-6


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Compound 10 Bound to Procaspase-6 within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:38.6 occ:0.50 F A:XMR301 0.0 38.6 0.5 C1 A:XMR301 1.4 40.4 0.5 C2 A:XMR301 2.4 40.2 0.5 C6 A:XMR301 2.4 39.5 0.5 C A:SER196 3.5 61.9 1.0 N A:SER196 3.5 63.5 1.0 CA A:SER196 3.6 62.4 1.0 C A:ALA195 3.6 57.8 1.0 C3 A:XMR301 3.7 41.8 0.5 C5 A:XMR301 3.7 41.8 0.5 O A:SER196 3.7 66.5 1.0 O A:ALA195 3.7 58.7 1.0 CA A:GLU214 3.8 71.0 1.0 N A:VAL197 3.9 58.9 1.0 O A:VAL197 3.9 67.8 1.0 CB A:ALA195 4.0 60.4 1.0 C4 A:XMR301 4.2 45.4 0.5 C A:VAL197 4.2 61.0 1.0 CB A:GLU214 4.2 77.9 1.0 N A:GLU214 4.3 68.9 1.0 CA A:ALA195 4.4 57.5 1.0 CG A:GLU214 4.5 82.7 1.0 N A:TYR198 4.7 56.5 1.0 CA A:VAL197 4.7 58.8 1.0 O1 A:XMR301 4.7 37.7 0.5 C A:ALA213 4.8 63.0 1.0 CD1 A:TYR198 5.0 57.5 1.0

Fluorine binding site 3 out of 4 in the Compound 10 Bound to Procaspase-6


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Compound 10 Bound to Procaspase-6 within 5.0Å range: probe atom residue distance (Å) B Occ C:F301 b:28.8 occ:0.50 F C:XMR301 0.0 28.8 0.5 C1 C:XMR301 1.3 30.8 0.5 C2 C:XMR301 2.4 31.0 0.5 C6 C:XMR301 2.4 31.3 0.5 C D:SER196 3.3 56.6 1.0 N D:SER196 3.3 57.4 1.0 O D:VAL197 3.4 58.8 1.0 N D:VAL197 3.5 54.6 1.0 CA D:SER196 3.5 59.6 1.0 C D:ALA195 3.5 58.9 1.0 C5 C:XMR301 3.6 33.7 0.5 C3 C:XMR301 3.6 33.4 0.5 O D:SER196 3.7 64.1 1.0 C D:VAL197 3.7 55.9 1.0 CB D:ALA195 3.8 62.1 1.0 O D:ALA195 3.9 56.6 1.0 CA D:GLU214 4.0 63.6 1.0 C4 C:XMR301 4.1 35.6 0.5 N D:GLU214 4.1 60.7 1.0 CA D:ALA195 4.2 61.1 1.0 CA D:VAL197 4.3 55.5 1.0 N D:TYR198 4.3 52.1 1.0 CB D:GLU214 4.5 69.7 1.0 C D:ALA213 4.6 55.7 1.0 O1 C:XMR301 4.7 33.8 0.5 O D:HOH304 4.8 45.2 1.0 CA D:TYR198 4.8 51.6 1.0 O D:ALA213 4.9 53.9 1.0 CD1 D:TYR198 4.9 56.1 1.0 CG D:GLU214 4.9 72.4 1.0

Fluorine binding site 4 out of 4 in the Compound 10 Bound to Procaspase-6


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Compound 10 Bound to Procaspase-6 within 5.0Å range: probe atom residue distance (Å) B Occ C:F301 b:28.5 occ:0.50 F C:XMR301 0.0 28.5 0.5 C1 C:XMR301 1.3 29.1 0.5 C2 C:XMR301 2.4 29.2 0.5 C6 C:XMR301 2.4 29.0 0.5 C C:SER196 3.3 58.4 1.0 N C:SER196 3.4 59.1 1.0 O C:VAL197 3.4 56.8 1.0 N C:VAL197 3.5 58.5 1.0 CA C:SER196 3.5 61.7 1.0 C C:ALA195 3.6 56.8 1.0 C5 C:XMR301 3.6 31.3 0.5 C3 C:XMR301 3.6 31.3 0.5 O C:SER196 3.6 58.1 1.0 C C:VAL197 3.8 56.3 1.0 CB C:ALA195 3.8 62.0 1.0 O C:ALA195 3.9 55.3 1.0 CA C:GLU214 3.9 57.4 1.0 C4 C:XMR301 4.1 33.2 0.5 N C:GLU214 4.1 54.3 1.0 CA C:ALA195 4.3 59.2 1.0 CA C:VAL197 4.3 55.7 1.0 N C:TYR198 4.3 53.8 1.0 CB C:GLU214 4.4 62.4 1.0 O C:HOH407 4.6 48.7 1.0 C C:ALA213 4.6 51.8 1.0 O1 C:XMR301 4.7 31.3 0.5 CA C:TYR198 4.8 52.7 1.0 CG C:GLU214 4.9 64.4 1.0 O C:ALA213 4.9 47.5 1.0 CD1 C:TYR198 4.9 53.1 1.0 O C:HOH425 4.9 55.8 1.0

P.Fan, Y.Zhao, A.R.Renslo, M.R.Arkin. A Comprehensive Empirical-Computational Study of Diverse Heteroarene Stacking Interactions Under Physiological Conditions To Be Published.