Chlorine in PDB 3eq0: Thrombin Inhibitor

All present enzymatic activity of Thrombin Inhibitor:
3.4.21.5;

The structure of Thrombin Inhibitor, PDB code: 3eq0 was solved by B.Baum, A.Heine, G.Klebe, T.Steinmetzer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.53
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.100, 71.400, 72.400, 90.00, 100.40, 90.00
R / Rfree (%)	19.6 / 24.9

The structure of Thrombin Inhibitor also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Thrombin Inhibitor (pdb code 3eq0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Thrombin Inhibitor, PDB code: 3eq0:

Chlorine binding site 1 out of 1 in the Thrombin Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Thrombin Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl901 b:15.5 occ:1.00 CL1 H:2TS901 0.0 15.5 1.0 C2 H:2TS901 1.8 13.2 1.0 C3 H:2TS901 2.8 15.3 1.0 C7 H:2TS901 2.8 14.9 1.0 O H:PHE227 3.3 12.6 1.0 O H:TRP215 3.4 10.3 1.0 CG1 H:VAL213 3.7 10.8 1.0 N H:PHE227 3.7 8.5 1.0 N H:TRP215 3.8 12.8 1.0 N H:SER214 3.9 8.5 1.0 CA H:GLY226 3.9 16.2 1.0 C H:TRP215 3.9 13.6 1.0 CB H:ALA190 3.9 14.6 1.0 CZ H:TYR228 4.0 12.8 1.0 C6 H:2TS901 4.1 14.3 1.0 C4 H:2TS901 4.1 15.5 1.0 C H:PHE227 4.1 8.8 1.0 C H:GLY226 4.1 9.5 1.0 CE2 H:TYR228 4.1 11.1 1.0 OH H:TYR228 4.2 13.9 1.0 CA H:TRP215 4.3 11.3 1.0 CE1 H:TYR228 4.3 11.5 1.0 C H:SER214 4.4 13.2 1.0 CA H:VAL213 4.4 6.0 1.0 CA H:PHE227 4.5 12.2 1.0 C H:VAL213 4.5 7.8 1.0 OD1 H:ASP189 4.5 16.8 1.0 C5 H:2TS901 4.6 11.7 1.0 CB H:VAL213 4.6 11.0 1.0 CD2 H:TYR228 4.6 8.8 1.0 N H:GLY216 4.6 14.3 1.0 CA H:SER214 4.7 9.6 1.0 CD1 H:TYR228 4.8 9.6 1.0 O H:HOH1005 4.9 12.9 1.0 CG H:TYR228 4.9 10.8 1.0

B.Baum, T.Steinmetzer, A.Heine, G.Klebe. Thrombin Inhibition To Be Published.