Chlorine in PDB 5kn1: Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form

The structure of Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form, PDB code: 5kn1 was solved by K.M.Lewis, S.Byrd, C.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.63 / 2.14
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	135.669, 165.604, 156.626, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 20.1

The structure of Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form also contains other interesting chemical elements:

Calcium

(Ca)

40 atoms

The binding sites of Chlorine atom in the Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form (pdb code 5kn1). 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 Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form, PDB code: 5kn1:

Chlorine binding site 1 out of 1 in the Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Recombinant Bovine Skeletal Calsequestrin, High-CA2+ Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl416 b:91.0 occ:1.00 O B:HOH567 2.1 75.6 1.0 O B:HOH592 2.1 59.5 1.0 H B:LEU246 3.3 0.7 1.0 CA B:CA409 3.4 72.5 1.0 HH12 B:ARG227 3.6 87.3 1.0 HB2 B:LEU246 3.7 96.7 1.0 OD1 B:ASP245 3.7 75.8 1.0 HG B:LEU246 3.9 99.9 1.0 H B:ASP247 4.0 0.9 1.0 N B:LEU246 4.0 84.7 1.0 HA B:ASP245 4.1 96.9 1.0 HH22 B:ARG227 4.1 98.8 1.0 NH1 B:ARG227 4.1 72.8 1.0 CG B:ASP245 4.2 80.0 1.0 OD2 B:ASP245 4.3 73.8 1.0 CB B:LEU246 4.4 80.6 1.0 HH11 B:ARG227 4.5 87.3 1.0 HD12 B:LEU246 4.5 1.0 1.0 NH2 B:ARG227 4.5 82.3 1.0 CG B:LEU246 4.6 83.2 1.0 CZ B:ARG227 4.6 79.4 1.0 OD1 B:ASP247 4.7 85.2 1.0 OD2 B:ASP247 4.8 84.1 1.0 CA B:ASP245 4.8 80.7 1.0 N B:ASP247 4.8 91.6 1.0 CA B:LEU246 4.8 85.4 1.0 C B:ASP245 4.8 76.1 1.0 CG B:ASP247 4.9 87.1 1.0

K.M.Lewis, G.R.Munske, S.S.Byrd, J.Kang, H.J.Cho, E.Rios, C.Kang. Characterization of Post-Translational Modifications to Calsequestrins of Cardiac and Skeletal Muscle. Int J Mol Sci V. 17 2016.
ISSN: ESSN 1422-0067
PubMed: 27649144
DOI: 10.3390/IJMS17091539