Sodium in PDB 6w3v: Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine

The structure of Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine, PDB code: 6w3v was solved by M.F.Khan, M.A.Machuca, M.M.Rahman, A.Roujeinikova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.85 / 1.47
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.396, 137.359, 48.759, 90.00, 93.96, 90.00
R / Rfree (%)	13.6 / 14.8

The structure of Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine (pdb code 6w3v). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine, PDB code: 6w3v:

Sodium binding site 1 out of 1 in the Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Ligand-Binding Domain of Campylobacter Jejuni Chemoreceptor TLP3 in Complex with L-Phenylalanine within 5.0Å range: probe atom residue distance (Å) B Occ B:Na302 b:19.7 occ:1.00 OG1 B:THR226 2.2 27.9 1.0 OG1 B:THR209 2.3 20.8 1.0 O B:GLY211 2.3 17.3 1.0 O B:THR209 2.5 23.8 1.0 OG1 B:THR213 2.5 17.5 1.0 O B:PRO210 2.6 23.1 1.0 C B:THR209 3.1 24.1 1.0 C B:PRO210 3.2 21.0 1.0 CB B:THR226 3.4 23.9 1.0 C B:GLY211 3.4 18.0 1.0 CB B:THR209 3.4 23.0 1.0 N B:THR213 3.6 16.2 1.0 CB B:THR213 3.6 14.3 1.0 CA B:THR209 3.7 27.0 1.0 N B:GLY211 3.8 18.6 1.0 N B:PRO210 3.8 21.7 1.0 CG2 B:THR226 3.8 26.2 1.0 O B:HOH485 3.9 17.9 1.0 O B:VAL206 3.9 26.5 1.0 CG2 B:THR213 3.9 15.5 1.0 CA B:PRO210 3.9 23.7 1.0 CA B:GLY211 4.0 19.1 1.0 CA B:THR213 4.1 15.5 1.0 N B:THR209 4.2 26.5 1.0 OG1 B:THR61 4.4 17.4 1.0 O B:THR213 4.4 19.6 1.0 N B:ASN212 4.4 16.3 1.0 CA B:THR226 4.6 21.7 1.0 C B:ASN212 4.7 16.3 1.0 C B:THR213 4.7 14.6 1.0 O B:ALA207 4.7 27.0 1.0 O B:HOH512 4.7 38.9 1.0 CG2 B:THR209 4.7 22.8 1.0 CA B:ASN212 4.7 14.9 1.0 CD B:PRO210 4.9 26.2 1.0 N B:THR226 5.0 20.9 1.0

M.F.Khan, M.A.Machuca, M.M.Rahman, C.Koc, R.S.Norton, B.J.Smith, A.Roujeinikova. Structure-Activity Relationship Study Reveals the Molecular Basis For Specific Sensing of Hydrophobic Amino Acids By the Campylobacter Jejuni Chemoreceptor TLP3 Biomolecules 2020.
ISSN: ESSN 2218-273X
DOI: 10.3390/BIOM10050744