Fluorine in PDB 2w3i: Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2

All present enzymatic activity of Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2:
3.4.21.6;

The structure of Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2, PDB code: 2w3i was solved by E.Zhang, I.Mochalkin, A.Casimiro-Garcia, C.A.Van Huis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.298, 72.688, 77.685, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 26.1

The structure of Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2 also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Fluorine atom in the Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2 (pdb code 2w3i). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2, PDB code: 2w3i:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1246 b:44.9 occ:1.00 F2 A:L1C1246 0.0 44.9 1.0 C14 A:L1C1246 1.3 44.3 1.0 C13 A:L1C1246 2.4 44.2 1.0 C15 A:L1C1246 2.4 44.0 1.0 OE2 A:GLU147 3.4 43.6 1.0 C18 A:L1C1246 3.6 43.9 1.0 C16 A:L1C1246 3.7 44.1 1.0 CG A:GLU147 3.7 43.5 1.0 CG A:LYS148 3.9 44.2 1.0 CD A:GLU147 4.0 43.2 1.0 C17 A:L1C1246 4.2 43.3 1.0 O A:GLU147 4.4 44.0 1.0 CB A:GLU147 4.5 43.9 1.0 C A:GLU147 4.5 44.0 1.0 CE A:LYS148 4.6 43.9 1.0 F1 A:L1C1246 4.7 44.8 1.0 N A:LYS148 4.8 44.2 1.0 CA A:LYS148 4.8 44.2 1.0 CD A:LYS148 4.8 44.0 1.0 CB A:LYS148 4.9 44.1 1.0 NH2 A:ARG222 5.0 38.0 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Fxa in Complex with 4,4-Disubstituted Pyrrolidine-1,2-Dicarboxamide Inhibitor 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1246 b:44.8 occ:1.00 F1 A:L1C1246 0.0 44.8 1.0 C16 A:L1C1246 1.3 44.1 1.0 C15 A:L1C1246 2.3 44.0 1.0 C17 A:L1C1246 2.4 43.3 1.0 C8 A:L1C1246 2.9 42.2 1.0 C11 A:L1C1246 3.1 40.5 1.0 C9 A:L1C1246 3.1 41.6 1.0 C14 A:L1C1246 3.6 44.3 1.0 C18 A:L1C1246 3.6 43.9 1.0 CB A:GLN192 3.8 37.3 1.0 N2 A:L1C1246 3.8 40.0 1.0 C10 A:L1C1246 3.9 41.1 1.0 OE1 A:GLN192 3.9 43.3 1.0 NH1 A:ARG143 4.0 40.4 1.0 O A:GLU147 4.0 44.0 1.0 CD A:GLN192 4.1 41.2 1.0 C13 A:L1C1246 4.1 44.2 1.0 CZ A:ARG143 4.3 40.4 1.0 O3 A:L1C1246 4.3 40.5 1.0 NE2 A:GLN192 4.4 42.6 1.0 CG A:GLN192 4.5 38.9 1.0 SG A:CYS220 4.6 35.6 1.0 F2 A:L1C1246 4.7 44.9 1.0 NE A:ARG143 4.7 40.1 1.0 CG A:GLU147 4.7 43.5 1.0 NH2 A:ARG143 4.8 41.2 1.0 C12 A:L1C1246 4.8 35.2 1.0 SG A:CYS191 4.9 35.5 1.0 CD A:ARG143 4.9 39.5 1.0 N A:GLN192 4.9 36.3 1.0 C A:GLU147 5.0 44.0 1.0 CA A:GLN192 5.0 36.8 1.0

C.A.Van Huis, A.Casimiro-Garcia, C.F.Bigge, W.L.Cody, D.A.Dudley, K.J.Filipski, R.J.Heemstra, J.T.Kohrt, R.J.J.Leadley, L.S.Narasimhan, T.Mcclanahan, I.Mochalkin, M.Pamment, J.T.Peterson, V.Sahasrabudhe, R.P.Schaum, J.J.Edmunds. Exploration of 4,4-Disubstituted Pyrrolidine-1,2- Dicarboxamides As Potent, Orally Active Factor Xa Inhibitors with Extended Duration of Action. Bioorg.Med.Chem. V. 17 2501 2009.
ISSN: ISSN 0968-0896
PubMed: 19231206
DOI: 10.1016/J.BMC.2009.01.063