Fluorine in PDB 4x6h: Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors.

All present enzymatic activity of Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors.:
3.4.22.38;

The structure of Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors., PDB code: 4x6h was solved by J.Borisek, B.Mohar, M.Vizovisek, P.Sosnowski, D.Turk, B.Turk, M.Novic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.67 / 1.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.439, 54.551, 88.015, 90.00, 90.00, 90.00
R / Rfree (%)	15.5 / 16.6

The binding sites of Fluorine atom in the Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors. (pdb code 4x6h). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors., PDB code: 4x6h:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors. within 5.0Å range: probe atom residue distance (Å) B Occ A:F301 b:9.4 occ:1.00 F22 A:3XT301 0.0 9.4 1.0 F22 A:I37302 0.0 8.6 0.0 C17 A:3XT301 1.4 7.6 1.0 C17 A:I37302 1.4 8.2 0.0 C16 A:3XT301 2.4 8.0 1.0 C16 A:I37302 2.4 7.7 0.0 C18 A:3XT301 2.4 7.8 1.0 C18 A:I37302 2.4 8.3 0.0 N21 A:3XT301 2.7 9.7 1.0 N21 A:I37302 2.7 8.8 0.0 OD2 A:ASP61 3.0 7.9 1.0 CG A:ASP61 3.5 6.6 1.0 CB A:ASP61 3.6 7.6 1.0 C15 A:3XT301 3.6 7.2 1.0 C15 A:I37302 3.6 7.7 0.0 C19 A:3XT301 3.6 8.2 1.0 C19 A:I37302 3.6 8.0 0.0 O A:GLY64 3.8 10.3 1.0 C20 A:3XT301 4.1 7.8 1.0 C20 A:I37302 4.1 7.7 0.0 O A:GLY65 4.3 7.4 1.0 C A:GLY64 4.3 7.8 1.0 C A:GLY65 4.4 6.5 1.0 OD1 A:ASP61 4.5 7.9 1.0 CA A:GLY65 4.5 7.1 1.0 N A:GLY65 4.6 7.1 1.0 C13 A:3XT301 4.8 7.5 1.0 C13 A:I37302 4.8 7.8 0.0 CA A:ASP61 4.9 6.8 1.0 O14 A:3XT301 5.0 8.4 1.0 O14 A:I37302 5.0 8.0 0.0

Fluorine binding site 2 out of 2 in the Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Development of N-(Functionalized Benzoyl)-Homocycloleucyl- Glycinonitriles As Potent Cathepsin K Inhibitors. within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:8.6 occ:0.00 F22 A:I37302 0.0 8.6 0.0 F22 A:3XT301 0.0 9.4 1.0 C17 A:3XT301 1.4 7.6 1.0 C17 A:I37302 1.4 8.2 0.0 C16 A:3XT301 2.4 8.0 1.0 C18 A:3XT301 2.4 7.8 1.0 C16 A:I37302 2.4 7.7 0.0 C18 A:I37302 2.4 8.3 0.0 N21 A:3XT301 2.7 9.7 1.0 N21 A:I37302 2.7 8.8 0.0 OD2 A:ASP61 3.0 7.9 1.0 CG A:ASP61 3.5 6.6 1.0 CB A:ASP61 3.6 7.6 1.0 C15 A:3XT301 3.6 7.2 1.0 C15 A:I37302 3.6 7.7 0.0 C19 A:3XT301 3.6 8.2 1.0 C19 A:I37302 3.6 8.0 0.0 O A:GLY64 3.8 10.3 1.0 C20 A:3XT301 4.1 7.8 1.0 C20 A:I37302 4.1 7.7 0.0 O A:GLY65 4.3 7.4 1.0 C A:GLY64 4.3 7.8 1.0 C A:GLY65 4.4 6.5 1.0 OD1 A:ASP61 4.5 7.9 1.0 CA A:GLY65 4.5 7.1 1.0 N A:GLY65 4.6 7.1 1.0 C13 A:3XT301 4.8 7.5 1.0 C13 A:I37302 4.8 7.8 0.0 CA A:ASP61 4.9 6.8 1.0 O14 A:3XT301 5.0 8.4 1.0 O14 A:I37302 5.0 8.0 0.0

J.Borisek, M.Vizovisek, P.Sosnowski, B.Turk, D.Turk, B.Mohar, M.Novic. Development of N-(Functionalized Benzoyl)-Homocycloleucyl-Glycinonitriles As Potent Cathepsin K Inhibitors. J.Med.Chem. V. 58 6928 2015.
ISSN: ISSN 0022-2623
PubMed: 26280490
DOI: 10.1021/ACS.JMEDCHEM.5B00746