Chlorine in PDB 6dtm: Crystal Structure of Helicobacter Pylori Tlpa Chemoreceptor Ligand Binding Domain

The structure of Crystal Structure of Helicobacter Pylori Tlpa Chemoreceptor Ligand Binding Domain, PDB code: 6dtm was solved by S.J.Remington, K.Guillemin, E.Sweeney, A.Perkins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.34 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	143.220, 67.830, 29.415, 90.00, 94.05, 90.00
R / Rfree (%)	22.2 / 32.3

The binding sites of Chlorine atom in the Crystal Structure of Helicobacter Pylori Tlpa Chemoreceptor Ligand Binding Domain (pdb code 6dtm). 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 Helicobacter Pylori Tlpa Chemoreceptor Ligand Binding Domain, PDB code: 6dtm:

Chlorine binding site 1 out of 1 in the Crystal Structure of Helicobacter Pylori Tlpa Chemoreceptor Ligand Binding Domain


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 Helicobacter Pylori Tlpa Chemoreceptor Ligand Binding Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:24.0 occ:1.00 NE1 A:TRP282 3.1 24.3 1.0 N A:VAL207 3.4 16.9 1.0 CE A:LYS147 3.5 48.9 1.0 CG2 A:VAL207 3.6 33.1 1.0 CG A:PRO150 3.7 15.2 1.0 NZ A:LYS147 3.7 42.5 1.0 CD A:PRO150 3.7 24.4 1.0 CB A:VAL207 3.9 38.3 1.0 CA A:GLY206 3.9 20.0 1.0 CD1 A:TRP282 4.0 18.3 1.0 CE2 A:TRP282 4.0 22.0 1.0 C A:GLY206 4.2 14.5 1.0 CZ2 A:TRP282 4.2 23.0 1.0 CD1 A:LEU212 4.3 12.9 1.0 CA A:VAL207 4.3 32.3 1.0 CD2 A:LEU212 4.6 15.3 1.0 CG1 A:VAL164 4.7 14.6 1.0 N A:PRO150 4.9 19.9 1.0 CD A:LYS147 4.9 38.5 1.0 CG A:LEU212 5.0 18.0 1.0

E.G.Sweeney, A.Perkins, K.Kallio, S.James Remington, K.Guillemin. Structures of the Ligand-Binding Domain of Helicobacter Pylori Chemoreceptor Tlpa. Protein Sci. V. 27 1961 2018.
ISSN: ESSN 1469-896X
PubMed: 30171638
DOI: 10.1002/PRO.3503