Chlorine in PDB 6gfs: Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine B-Lactoglobulin

The structure of Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine B-Lactoglobulin, PDB code: 6gfs was solved by G.Kontopidis, M.Rovoli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.80 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.277, 53.277, 111.091, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 24.8

The binding sites of Chlorine atom in the Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine B-Lactoglobulin (pdb code 6gfs). 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 Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine B-Lactoglobulin, PDB code: 6gfs:

Chlorine binding site 1 out of 1 in the Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine B-Lactoglobulin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine B-Lactoglobulin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:63.4 occ:0.70 N A:LYS77 3.1 46.2 1.0 CD A:LYS77 3.5 66.3 1.0 CB A:THR76 3.6 41.4 1.0 CE A:LYS77 3.6 68.7 1.0 CA A:THR76 3.7 43.1 1.0 CB A:LYS77 3.8 54.0 1.0 C A:THR76 3.9 44.3 1.0 CA A:LYS77 4.1 49.6 1.0 CG A:LYS77 4.2 60.9 1.0 CG2 A:THR76 4.3 41.5 1.0 NZ A:LYS77 4.3 72.3 1.0 O A:HOH342 4.4 15.9 0.5 OG1 A:THR76 4.6 39.3 1.0

M.Rovoli, T.Thireou, Y.Choiset, T.Haertle, L.Sawyer, E.Eliopoulos, G.Kontopidis. Thermodynamic, Crystallographic and Computational Studies of Non-Mammalian Fatty Acid Binding to Bovine Beta-Lactoglobulin. Int. J. Biol. Macromol. V. 118 296 2018.
ISSN: ISSN 1879-0003
PubMed: 29879410
DOI: 10.1016/J.IJBIOMAC.2018.05.226