Chlorine in PDB 2zgb: Thrombin Inhibition

All present enzymatic activity of Thrombin Inhibition:
3.4.21.5;

The structure of Thrombin Inhibition, PDB code: 2zgb was solved by B.Baum, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.760, 71.370, 72.570, 90.00, 100.28, 90.00
R / Rfree (%)	19.8 / 24.2

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

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Thrombin Inhibition (pdb code 2zgb). 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 Inhibition, PDB code: 2zgb:

Chlorine binding site 1 out of 1 in the Thrombin Inhibition


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Thrombin Inhibition within 5.0Å range: probe atom residue distance (Å) B Occ H:Cl1801 b:17.8 occ:1.00 CL21 H:21U1801 0.0 17.8 1.0 C29 H:21U1801 1.8 15.0 1.0 C28 H:21U1801 2.7 23.0 1.0 C30 H:21U1801 2.7 17.9 1.0 O H:PHE227 3.3 14.6 1.0 O H:TRP215 3.3 14.3 1.0 N H:PHE227 3.6 12.3 1.0 CG1 H:VAL213 3.6 10.6 1.0 CA H:GLY226 3.7 14.4 1.0 N H:TRP215 3.8 17.0 1.0 C H:TRP215 3.8 18.9 1.0 N H:SER214 3.9 11.5 1.0 CB H:ALA190 4.0 15.7 1.0 C27 H:21U1801 4.0 17.1 1.0 C H:GLY226 4.0 11.7 1.0 C25 H:21U1801 4.0 16.8 1.0 CZ H:TYR228 4.1 13.0 1.0 C H:PHE227 4.2 13.9 1.0 OH H:TYR228 4.3 16.8 1.0 CA H:TRP215 4.3 17.4 1.0 CE2 H:TYR228 4.3 12.9 1.0 C H:SER214 4.4 14.9 1.0 CE1 H:TYR228 4.4 12.0 1.0 CA H:PHE227 4.5 15.1 1.0 C26 H:21U1801 4.5 15.9 1.0 CA H:VAL213 4.5 8.7 1.0 OD1 H:ASP189 4.6 18.3 1.0 C H:VAL213 4.6 13.3 1.0 N H:GLY216 4.6 16.1 1.0 CB H:VAL213 4.7 10.6 1.0 CA H:SER214 4.7 10.9 1.0 CD2 H:TYR228 4.8 10.6 1.0 CD1 H:TYR228 4.9 14.0 1.0 O H:HOH2001 5.0 13.9 1.0

B.Baum, L.Muley, M.Smolinski, A.Heine, D.Hangauer, G.Klebe. Non-Additivity of Functional Group Contributions in Protein-Ligand Binding: A Comprehensive Study By Crystallography and Isothermal Titration Calorimetry. J.Mol.Biol. V. 397 1042 2010.
ISSN: ISSN 0022-2836
PubMed: 20156458
DOI: 10.1016/J.JMB.2010.02.007