Chlorine in PDB 2xu5: Cathepsin L with A Nitrile Inhibitor

All present enzymatic activity of Cathepsin L with A Nitrile Inhibitor:
3.4.22.15;

The structure of Cathepsin L with A Nitrile Inhibitor, PDB code: 2xu5 was solved by D.W.Banner, J.M.Benz, W.Haap, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.90 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.943, 59.107, 89.790, 90.00, 90.00, 90.00
R / Rfree (%)	21.691 / 27.583

The binding sites of Chlorine atom in the Cathepsin L with A Nitrile Inhibitor (pdb code 2xu5). 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 Cathepsin L with A Nitrile Inhibitor, PDB code: 2xu5:

Chlorine binding site 1 out of 1 in the Cathepsin L with A Nitrile Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cathepsin L with A Nitrile Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1221 b:39.8 occ:1.00 CL A:XU51221 0.0 39.8 1.0 C16 A:XU51221 1.7 25.1 1.0 C17 A:XU51221 2.7 23.6 1.0 C15 A:XU51221 2.7 22.0 1.0 O22 A:XU51221 2.9 20.4 1.0 O A:HOH2049 3.1 22.7 1.0 S14 A:XU51221 3.2 21.4 1.0 C12 A:XU51221 3.4 19.4 1.0 CE A:MET70 3.6 18.5 1.0 SD A:MET70 3.8 21.7 1.0 CD2 A:LEU69 3.9 25.3 1.0 C18 A:XU51221 3.9 23.2 1.0 C20 A:XU51221 3.9 23.1 1.0 O A:HOH2050 4.0 29.2 1.0 O A:HOH2139 4.1 29.4 1.0 CB A:ALA135 4.1 15.5 1.0 C19 A:XU51221 4.4 25.0 1.0 N A:MET70 4.4 19.9 1.0 CB A:ALA214 4.4 20.6 1.0 O23 A:XU51221 4.5 20.1 1.0 C11 A:XU51221 4.5 21.9 1.0 CA A:LEU69 4.5 24.2 1.0 CB A:LEU69 4.6 19.5 1.0 O A:ALA214 4.6 24.4 1.0 C13 A:XU51221 4.6 19.4 1.0 CG A:LEU69 4.8 25.9 1.0 CA A:ALA135 4.9 15.4 1.0

L.A.Hardegger, B.Kuhn, B.Spinnler, L.Anselm, R.Ecabert, M.Stihle, B.Gsell, R.Thoma, J.Diez, J.Benz, J.M.Plancher, G.Hartmann, D.W.Banner, W.Haap, F.Diederich. Systematic Investigation of Halogen Bonding in Protein-Ligand Interactions. Angew.Chem.Int.Ed.Engl. V. 50 314 2011.
ISSN: ISSN 1433-7851
PubMed: 21184410
DOI: 10.1002/ANIE.201006781