Chlorine in PDB 5qci: Crystal Structure of Human Cathepsin-S with Bound Ligand

All present enzymatic activity of Crystal Structure of Human Cathepsin-S with Bound Ligand:
3.4.22.27;

The structure of Crystal Structure of Human Cathepsin-S with Bound Ligand, PDB code: 5qci was solved by S.D.Bembenek, M.K.Ameriks, T.Mirzadegan, H.Yang, C.Shao, S.K.Burley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.04 / 2.18
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	78.505, 73.542, 44.655, 90.00, 103.86, 90.00
R / Rfree (%)	15.8 / 19.3

The binding sites of Chlorine atom in the Crystal Structure of Human Cathepsin-S with Bound Ligand (pdb code 5qci). 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 Crystal Structure of Human Cathepsin-S with Bound Ligand, PDB code: 5qci:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human Cathepsin-S with Bound Ligand


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Cathepsin-S with Bound Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl803 b:26.0 occ:1.00 CL6 A:BJV803 0.0 26.0 1.0 C51 A:BJV803 1.7 26.4 1.0 C52 A:BJV803 2.7 23.1 1.0 C50 A:BJV803 2.7 20.5 1.0 C62 A:BJV803 3.1 23.8 1.0 N A:GLY165 3.4 13.2 1.0 CA A:GLY165 3.6 13.8 1.0 C A:HIS164 3.7 12.7 1.0 C64 A:BJV803 3.9 25.1 1.0 SD A:MET71 4.0 14.3 1.0 C53 A:BJV803 4.0 19.8 1.0 C49 A:BJV803 4.0 20.3 1.0 O A:HIS164 4.1 11.9 1.0 CE A:MET71 4.2 16.9 1.0 N A:HIS164 4.2 14.1 1.0 O A:HOH1040 4.3 25.2 1.0 CA A:HIS164 4.4 10.8 1.0 CA A:GLY137 4.4 11.7 1.0 O A:GLY69 4.4 16.6 1.0 C39 A:BJV803 4.5 19.4 1.0 OG A:SER25 4.8 14.0 1.0 C A:ASN163 4.9 16.7 1.0 CB A:TRP26 4.9 12.5 1.0 O A:HOH932 4.9 20.1 1.0

S.D.Bembenek, M.K.Ameriks, T.Mirzadegan, H.Yang, C.Shao, S.K.Burley. Crystal Structure of Human Cathepsin-S with Bound Ligand To Be Published.