Chlorine in PDB 5lk5: Crystal Structure of the Globular Domain of Human Calreticulin Mutant D71K

The structure of Crystal Structure of the Globular Domain of Human Calreticulin Mutant D71K, PDB code: 5lk5 was solved by C.Gaboriaud, G.Cioci, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.77 / 2.30
Space group	P 42
Cell size a, b, c (Å), α, β, γ (°)	196.976, 196.976, 67.806, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 24.7

The structure of Crystal Structure of the Globular Domain of Human Calreticulin Mutant D71K also contains other interesting chemical elements:

Calcium

(Ca)

10 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Globular Domain of Human Calreticulin Mutant D71K (pdb code 5lk5). 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 the Globular Domain of Human Calreticulin Mutant D71K, PDB code: 5lk5:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Globular Domain of Human Calreticulin Mutant D71K


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 the Globular Domain of Human Calreticulin Mutant D71K within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl402 b:31.9 occ:1.00 N E:LEU51 3.3 21.2 1.0 CB E:LEU51 3.9 21.7 1.0 CA E:VAL50 4.1 19.1 1.0 CZ2 E:TRP33 4.1 15.6 1.0 CA E:LEU51 4.2 22.2 1.0 C E:VAL50 4.2 20.1 1.0 CG1 E:VAL50 4.3 22.9 1.0 CB E:VAL50 4.5 20.9 1.0 OD1 E:ASP31 4.6 65.7 1.0 CG2 E:VAL50 4.6 20.4 1.0 O E:LEU51 4.6 23.5 1.0 NE1 E:TRP33 4.7 16.0 1.0 CE2 E:TRP33 4.8 16.2 1.0 C E:LEU51 4.9 21.9 1.0

C.Moreau, G.Cioci, M.Iannello, E.Laffly, A.Chouquet, A.Ferreira, N.M.Thielens, C.Gaboriaud. Structures of Parasite Calreticulins Provide Insights Into Their Flexibility and Dual Carbohydrate/Peptide-Binding Properties. Iucrj V. 3 408 2016.
ISSN: ESSN 2052-2525
PubMed: 27840680
DOI: 10.1107/S2052252516012847