Chlorine in PDB 2bxt: Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker

All present enzymatic activity of Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker:
3.4.21.5;

The structure of Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker, PDB code: 2bxt was solved by S.Bulat, S.Bosio, E.Grabowski, M.A.Papadopoulos, S.Cerezo-Galvez, C.Rosenbaum, V.G.Matassa, I.Ott, G.Metz, J.Schamberger, R.Sekul, A.Feurer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.83
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.505, 71.917, 72.522, 90.00, 100.35, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker (pdb code 2bxt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker, PDB code: 2bxt:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl1246 b:27.0 occ:1.00 CL2 H:C2D1246 0.0 27.0 1.0 C6 H:C2D1246 1.7 28.5 1.0 C8 H:C2D1246 2.7 29.7 1.0 C4 H:C2D1246 2.8 30.4 1.0 O H:PHE227 3.3 16.9 1.0 O H:TRP215 3.4 21.7 1.0 N H:PHE227 3.6 17.1 1.0 CG1 H:VAL213 3.6 17.7 1.0 CA H:GLY226 3.6 19.1 1.0 C H:TRP215 3.9 20.9 1.0 C H:GLY226 3.9 18.4 1.0 N H:TRP215 4.0 19.5 1.0 C9 H:C2D1246 4.0 27.7 1.0 CB H:ALA190 4.0 21.9 1.0 CZ H:TYR228 4.1 16.3 1.0 C5 H:C2D1246 4.1 30.1 1.0 N H:SER214 4.1 17.4 1.0 OH H:TYR228 4.2 18.4 1.0 C H:PHE227 4.2 15.8 1.0 CE2 H:TYR228 4.3 18.0 1.0 CE1 H:TYR228 4.4 19.6 1.0 CA H:TRP215 4.4 21.1 1.0 CA H:PHE227 4.5 16.9 1.0 CA H:VAL213 4.6 17.5 1.0 C7 H:C2D1246 4.6 30.6 1.0 OD1 H:ASP189 4.6 23.1 1.0 N H:GLY216 4.7 20.1 1.0 CB H:VAL213 4.7 18.2 1.0 C H:SER214 4.7 19.6 1.0 C H:VAL213 4.7 18.3 1.0 O H:HOH2114 4.8 22.5 1.0 CD2 H:TYR228 4.9 17.3 1.0 CD1 H:TYR228 4.9 19.9 1.0 O H:GLY226 4.9 17.1 1.0 CA H:SER214 5.0 18.5 1.0

Chlorine binding site 2 out of 2 in the Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Design and Discovery of Novel, Potent Thrombin Inhibitors with A Solubilizing Cationic P1-P2-Linker within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl1246 b:31.1 occ:1.00 CL3 H:C2D1246 0.0 31.1 1.0 C17 H:C2D1246 1.7 30.6 1.0 C19 H:C2D1246 2.7 29.5 1.0 N18 H:C2D1246 2.7 29.1 1.0 C16 H:C2D1246 3.1 30.3 1.0 CE2 H:TYR60A 3.6 26.4 1.0 CZ H:TYR60A 3.6 25.7 1.0 CD2 H:TYR60A 3.7 25.1 1.0 CE1 H:TYR60A 3.8 25.0 1.0 C15 H:C2D1246 3.8 34.2 1.0 CD2 H:HIS57 3.8 24.6 1.0 CG H:TYR60A 3.9 22.5 1.0 CD1 H:TYR60A 3.9 25.0 1.0 CH2 H:TRP60D 3.9 46.6 1.0 CD1 H:LEU99 3.9 28.9 1.0 CG H:HIS57 4.0 22.3 1.0 CZ3 H:TRP60D 4.0 48.0 1.0 CB H:HIS57 4.0 21.7 1.0 C20 H:C2D1246 4.0 30.1 1.0 N21 H:C2D1246 4.1 31.9 1.0 OH H:TYR60A 4.3 25.2 1.0 CD2 H:LEU99 4.4 28.8 1.0 CZ2 H:TRP60D 4.4 48.9 1.0 C22 H:C2D1246 4.6 28.9 1.0 NE2 H:HIS57 4.6 27.1 1.0 CE3 H:TRP60D 4.6 48.4 1.0 CG H:LEU99 4.7 30.4 1.0 CB H:TYR60A 4.7 24.0 1.0 ND1 H:HIS57 4.8 21.0 1.0 CE2 H:TRP60D 5.0 50.1 1.0

S.Bulat, S.Bosio, M.A.Papadopoulos, S.Cerezo-Galvez, E.Grabowski, C.Rosenbaum, V.G.Matassa, I.Ott, G.Metz, J.Schamberger, R.Sekul, A.Feurer. Design and Discovery of Novel, Potent Pyrazinone-Based Thrombin Inhibitors with A Solubilizing P1-P2-Linker Lett.Drug Des.Discovery V. 3 289 2006.
ISSN: ISSN 1570-1808
DOI: 10.2174/157018006777574203