Fluorine in PDB 2g24: Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring

All present enzymatic activity of Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring:
3.4.23.15;

The structure of Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring, PDB code: 2g24 was solved by D.D.Holsworth, M.Jalaiea, E.Zhanga, P.Mcconnella, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	140.885, 140.885, 140.885, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 27

The binding sites of Fluorine atom in the Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring (pdb code 2g24). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring, PDB code: 2g24:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring within 5.0Å range: probe atom residue distance (Å) B Occ A:F334 b:40.0 occ:1.00 F1 A:7IG334 0.0 40.0 1.0 C13 A:7IG334 1.4 43.9 1.0 C14 A:7IG334 2.4 42.9 1.0 C18 A:7IG334 2.4 44.8 1.0 CG2 A:THR80 3.3 22.1 1.0 CB A:THR80 3.4 21.8 1.0 C17 A:7IG334 3.7 45.9 1.0 C15 A:7IG334 3.7 42.1 1.0 OG1 A:THR80 3.9 23.9 1.0 O A:HOH358 4.1 40.0 1.0 C16 A:7IG334 4.2 42.9 1.0 CB A:PRO113 4.6 23.8 1.0 CA A:THR80 4.7 24.4 1.0 F2 A:7IG334 4.8 49.4 1.0 O A:THR80 4.8 23.6 1.0 C19 A:7IG334 5.0 39.9 1.0

Fluorine binding site 2 out of 2 in the Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Ketopiperazine-Based Renin Inhibitors: Optimization of the "C" Ring within 5.0Å range: probe atom residue distance (Å) B Occ A:F334 b:49.4 occ:1.00 F2 A:7IG334 0.0 49.4 1.0 C17 A:7IG334 1.3 45.9 1.0 C16 A:7IG334 2.4 42.9 1.0 C18 A:7IG334 2.4 44.8 1.0 CD1 A:LEU116 3.3 29.3 1.0 CB A:LEU116 3.5 22.6 1.0 C13 A:7IG334 3.6 43.9 1.0 C15 A:7IG334 3.7 42.1 1.0 O A:HOH375 3.7 22.5 1.0 CG A:LEU116 4.0 26.6 1.0 C14 A:7IG334 4.1 42.9 1.0 O A:LEU116 4.5 20.3 1.0 F1 A:7IG334 4.8 40.0 1.0 CA A:LEU116 4.8 22.3 1.0 CD2 A:LEU116 4.9 28.3 1.0 C19 A:7IG334 4.9 39.9 1.0 C A:LEU116 5.0 22.6 1.0 NE2 A:GLN14 5.0 20.0 1.0

D.D.Holsworth, C.Cai, X.M.Cheng, W.L.Cody, D.M.Downing, N.Erasga, C.Lee, N.A.Powell, J.J.Ednunds, M.Stier, M.Jalaie, E.Zhang, P.Mcconnell, M.J.Ryan, J.Bryant, T.Li, A.Kasani, E.Hall, R.Subedi, M.Rahim, S.Maiti. Ketopiperazine-Based Renin Inhibitors: Optimization of the C Ring Bioorg.Med.Chem.Lett. V. 16 2500 2006.
ISSN: ISSN 0960-894X
PubMed: 16480874
DOI: 10.1016/J.BMCL.2006.01.084