Chlorine in PDB 2vwn: Aminopyrrolidine Factor Xa Inhibitor

All present enzymatic activity of Aminopyrrolidine Factor Xa Inhibitor:
3.4.21.6;

The structure of Aminopyrrolidine Factor Xa Inhibitor, PDB code: 2vwn was solved by K.Groebke-Zbinden, D.W.Banner, J.M.Benz, F.Blasco, G.Decoret, J.Himber, B.Kuhn, N.Panday, F.Ricklin, P.Risch, D.Schlatter, M.Stahl, R.Unger, W.Haap, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.54 / 1.61
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	105.540, 105.540, 49.790, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 22.8

The structure of Aminopyrrolidine Factor Xa Inhibitor also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Calcium	(Ca)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Chlorine atom in the Aminopyrrolidine Factor Xa Inhibitor (pdb code 2vwn). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Aminopyrrolidine Factor Xa Inhibitor, PDB code: 2vwn:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Aminopyrrolidine Factor Xa Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aminopyrrolidine Factor Xa Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1245 b:16.8 occ:1.00 CL1 A:H251245 0.0 16.8 1.0 C10 A:H251245 1.8 16.2 1.0 C19 A:H251245 2.8 15.9 1.0 S3 A:H251245 3.0 16.8 1.0 CZ A:TYR228 3.4 17.0 1.0 N A:ILE227 3.5 13.0 1.0 CE2 A:TYR228 3.6 13.2 1.0 CA A:GLY226 3.6 15.5 1.0 O A:ILE227 3.6 13.3 1.0 OH A:TYR228 3.6 18.4 1.0 CG1 A:VAL213 3.8 15.6 1.0 C A:GLY226 3.8 14.9 1.0 O A:TRP215 3.9 14.3 1.0 CB A:ALA190 3.9 17.7 1.0 CE1 A:TYR228 3.9 16.7 1.0 C12 A:H251245 4.0 15.1 1.0 C2 A:H251245 4.1 15.5 1.0 CD2 A:TYR228 4.2 13.4 1.0 C A:ILE227 4.2 13.0 1.0 O A:HOH2211 4.3 20.0 1.0 OD1 A:ASP189 4.4 19.9 1.0 N A:SER214 4.4 13.3 1.0 CD1 A:TYR228 4.5 14.5 1.0 CA A:ILE227 4.5 12.7 1.0 C A:TRP215 4.6 14.4 1.0 CG A:TYR228 4.6 12.3 1.0 N A:TRP215 4.6 12.9 1.0 CA A:VAL213 4.7 14.2 1.0 CB A:VAL213 4.7 14.6 1.0 O A:GLY226 4.7 15.2 1.0 CA A:ALA190 5.0 18.4 1.0 N A:GLY226 5.0 15.1 1.0 C A:VAL213 5.0 14.1 1.0

Chlorine binding site 2 out of 3 in the Aminopyrrolidine Factor Xa Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Aminopyrrolidine Factor Xa Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1248 b:26.1 occ:1.00 O A:HOH2052 2.9 46.9 1.0 N A:GLY218 3.2 17.5 1.0 N4 A:H251245 3.5 18.1 1.0 C22 A:H251245 3.6 20.6 1.0 C14 A:H251245 3.7 20.6 1.0 C31 A:H251245 3.8 20.1 1.0 N15 A:H251245 3.8 17.9 1.0 CA A:GLY218 4.0 18.1 1.0 C A:GLU217 4.1 17.4 1.0 CA A:GLU217 4.2 16.4 1.0 O A:GLY216 4.2 15.0 1.0 NH2 A:ARG222 4.4 30.6 1.0 O27 A:H251245 4.5 20.9 1.0 O A:HOH2133 4.6 45.9 1.0 C28 A:H251245 4.6 16.4 1.0 C16 A:H251245 4.6 19.2 1.0 C34 A:H251245 4.8 17.9 1.0 C20 A:H251245 4.9 18.3 1.0

Chlorine binding site 3 out of 3 in the Aminopyrrolidine Factor Xa Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Aminopyrrolidine Factor Xa Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1249 b:42.2 occ:1.00 N A:GLN178 3.0 18.6 1.0 CG A:GLN178 3.5 23.0 1.0 CA A:THR177 3.6 16.9 1.0 CB A:THR177 3.7 18.1 1.0 CB A:GLN178 3.7 21.2 1.0 C A:THR177 3.8 17.4 1.0 O A:HOH2096 3.9 38.7 1.0 CA A:GLN178 4.0 19.5 1.0 O A:HOH2162 4.2 25.8 1.0 CD A:GLN178 4.3 30.2 1.0 CG2 A:THR177 4.4 17.6 1.0 O A:HOH2171 4.4 25.0 1.0 OE1 A:GLN178 4.6 33.5 1.0 OG1 A:THR177 4.8 16.9 1.0 O A:HOH2170 4.8 19.1 1.0 O A:ILE176 4.9 16.3 1.0 N A:THR177 5.0 16.3 1.0 O A:THR177 5.0 16.3 1.0

K.G.Zbinden, L.Anselm, D.W.Banner, J.M.Benz, F.Blasco, G.Decoret, J.Himber, B.Kuhn, N.Panday, F.Ricklin, P.Risch, D.Schlatter, M.Stahl, S.Thomi, R.Unger, W.Haap. Design of Novel Aminopyrrolidine Factor Xa Inhibitors From A Screening Hit. Eur.J.Med.Chem. V. 44 2787 2009.
ISSN: ISSN 0223-5234
PubMed: 19200624
DOI: 10.1016/J.EJMECH.2008.12.025