Chlorine in PDB 3g6z: Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors

All present enzymatic activity of Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors:
3.4.23.15;

The structure of Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors, PDB code: 3g6z was solved by O.Bezencon, D.Bur, L.Prade, T.Weller, C.Boss, W.Fischli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.503, 94.751, 119.832, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25.8

The binding sites of Chlorine atom in the Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors (pdb code 3g6z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors, PDB code: 3g6z:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl342 b:51.4 occ:1.00 CL9 A:A7T342 0.0 51.4 1.0 C6 A:A7T342 1.8 51.3 1.0 C10 A:A7T342 2.8 52.0 1.0 C3 A:A7T342 2.9 50.5 1.0 O5 A:A7T342 3.1 48.4 1.0 CE2 A:PHE119 3.5 44.2 1.0 CG2 A:VAL127 3.6 32.0 1.0 C31 A:A7T342 3.6 36.0 1.0 C32 A:A7T342 3.7 35.3 1.0 CD2 A:PHE119 3.7 44.2 1.0 C8 A:A7T342 3.8 45.0 1.0 C14 A:A7T342 3.8 39.2 1.0 CE2 A:PHE124 3.9 28.4 1.0 O13 A:A7T342 3.9 40.6 1.0 C16 A:A7T342 3.9 39.9 1.0 C7 A:A7T342 4.1 51.0 1.0 C40 A:A7T342 4.1 35.5 1.0 N27 A:A7T342 4.1 35.9 1.0 C12 A:A7T342 4.2 41.7 1.0 C2 A:A7T342 4.2 51.7 1.0 C34 A:A7T342 4.2 35.6 1.0 C15 A:A7T342 4.3 38.3 1.0 CZ A:PHE124 4.3 29.1 1.0 C18 A:A7T342 4.5 39.6 1.0 C4 A:A7T342 4.7 51.2 1.0 C36 A:A7T342 4.7 35.5 1.0 CZ A:PHE119 4.8 44.7 1.0 C17 A:A7T342 4.8 36.8 1.0 C37 A:A7T342 4.9 35.4 1.0 C19 A:A7T342 5.0 38.4 1.0 C35 A:A7T342 5.0 36.2 1.0 CB A:VAL127 5.0 30.4 1.0

Chlorine binding site 2 out of 4 in the Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl342 b:52.2 occ:1.00 CL1 A:A7T342 0.0 52.2 1.0 C2 A:A7T342 1.8 51.7 1.0 C4 A:A7T342 2.7 51.2 1.0 C3 A:A7T342 2.9 50.5 1.0 O5 A:A7T342 3.2 48.4 1.0 CG2 A:VAL111 3.4 43.4 1.0 C8 A:A7T342 3.7 45.0 1.0 C A:VAL46 3.7 37.8 1.0 N A:PRO47 3.8 38.2 1.0 CA A:VAL46 3.8 37.0 1.0 CB A:TRP45 3.9 37.7 1.0 CB A:VAL111 3.9 43.3 1.0 N A:VAL46 4.0 36.2 1.0 O A:ASP125 4.0 32.8 1.0 C A:TRP45 4.0 36.6 1.0 CD A:PRO47 4.0 38.1 1.0 CG A:PRO47 4.0 38.2 1.0 C7 A:A7T342 4.0 51.0 1.0 O A:TRP45 4.2 36.1 1.0 O A:VAL46 4.2 38.4 1.0 C6 A:A7T342 4.2 51.3 1.0 CA A:PRO47 4.4 38.2 1.0 SD A:MET114 4.5 49.4 1.0 CA A:GLY126 4.5 32.3 1.0 CG1 A:VAL111 4.5 43.0 1.0 CA A:TRP45 4.6 36.2 1.0 C10 A:A7T342 4.6 52.0 1.0 CB A:PRO47 4.7 38.6 1.0 CG A:TRP45 4.9 39.1 1.0 C A:ASP125 5.0 32.7 1.0 C12 A:A7T342 5.0 41.7 1.0

Chlorine binding site 3 out of 4 in the Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl342 b:43.5 occ:1.00 CL9 B:A7T342 0.0 43.5 1.0 C6 B:A7T342 1.8 40.8 1.0 C3 B:A7T342 2.8 39.6 1.0 C10 B:A7T342 2.8 39.7 1.0 O5 B:A7T342 3.0 37.9 1.0 CG2 B:VAL127 3.3 24.6 1.0 CE1 B:PHE119 3.6 35.2 1.0 C31 B:A7T342 3.6 32.2 1.0 C32 B:A7T342 3.7 30.1 1.0 C34 B:A7T342 3.8 33.3 1.0 CD1 B:PHE119 3.8 33.3 1.0 C8 B:A7T342 3.9 34.6 1.0 C14 B:A7T342 3.9 31.0 1.0 CE2 B:PHE124 3.9 24.0 1.0 C15 B:A7T342 4.0 29.4 1.0 O13 B:A7T342 4.0 32.5 1.0 C7 B:A7T342 4.1 40.8 1.0 C2 B:A7T342 4.1 41.6 1.0 N27 B:A7T342 4.1 31.4 1.0 C40 B:A7T342 4.2 27.7 1.0 C12 B:A7T342 4.3 34.4 1.0 C16 B:A7T342 4.4 28.5 1.0 CZ B:PHE124 4.4 23.8 1.0 C17 B:A7T342 4.5 31.8 1.0 C4 B:A7T342 4.6 41.1 1.0 C36 B:A7T342 4.7 29.4 1.0 CB B:VAL127 4.7 22.3 1.0 CZ B:PHE119 4.9 32.3 1.0 C37 B:A7T342 4.9 28.9 1.0 C35 B:A7T342 4.9 33.5 1.0 C18 B:A7T342 4.9 29.8 1.0 C19 B:A7T342 5.0 29.6 1.0

Chlorine binding site 4 out of 4 in the Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Design and Preparation of Potent, Non-Peptidic, Bioavailable Renin Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl342 b:42.3 occ:1.00 CL1 B:A7T342 0.0 42.3 1.0 C2 B:A7T342 1.8 41.6 1.0 C4 B:A7T342 2.7 41.1 1.0 C3 B:A7T342 2.8 39.6 1.0 O5 B:A7T342 3.1 37.9 1.0 C8 B:A7T342 3.4 34.6 1.0 CG2 B:VAL111 3.4 23.3 1.0 C B:VAL46 3.7 24.9 1.0 N B:PRO47 3.8 24.6 1.0 CB B:VAL111 3.9 24.8 1.0 CA B:VAL46 3.9 25.1 1.0 C B:TRP45 4.0 26.6 1.0 CB B:TRP45 4.0 27.6 1.0 O B:TRP45 4.0 26.2 1.0 O B:ASP125 4.0 24.1 1.0 C7 B:A7T342 4.0 40.8 1.0 N B:VAL46 4.0 25.7 1.0 O B:VAL46 4.1 25.0 1.0 CD B:PRO47 4.1 25.4 1.0 C6 B:A7T342 4.1 40.8 1.0 CG B:PRO47 4.2 25.5 1.0 SD B:MET114 4.4 34.5 1.0 CA B:PRO47 4.5 25.0 1.0 CA B:GLY126 4.5 23.1 1.0 CG1 B:VAL111 4.5 25.0 1.0 C10 B:A7T342 4.6 39.7 1.0 CA B:TRP45 4.6 26.5 1.0 C12 B:A7T342 4.8 34.4 1.0 CB B:PRO47 4.9 24.9 1.0 CE B:MET114 4.9 36.6 1.0

O.Bezencon, D.Bur, T.Weller, S.Richard-Bildstein, L.Remen, T.Sifferlen, O.Corminboeuf, C.Grisostomi, C.Boss, L.Prade, S.Delahaye, A.Treiber, P.Strickner, C.Binkert, P.Hess, B.Steiner, W.Fischli. Design and Preparation of Potent, Nonpeptidic, Bioavailable Renin Inhibitors J.Med.Chem. V. 52 3689 2009.
ISSN: ISSN 0022-2623
PubMed: 19358611
DOI: 10.1021/JM900022F