Chlorine in PDB 6shu: Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine

The structure of Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine, PDB code: 6shu was solved by G.Guedez, M.Astrand, J.Cuellar, J.Hytonen, T.A.Salminen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.71 / 1.43
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.780, 42.900, 66.380, 90.00, 117.34, 90.00
R / Rfree (%)	15.4 / 17.9

The structure of Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine (pdb code 6shu). 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 Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine, PDB code: 6shu:

Chlorine binding site 1 out of 1 in the Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Borrelia Burgdorferi Bmpd Nucleoside Binding Protein Bound to Adenosine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:12.0 occ:1.00 O A:HOH618 3.0 19.0 1.0 NE A:ARG183 3.0 25.7 1.0 O A:HOH823 3.2 13.9 1.0 NH2 A:ARG183 3.8 26.2 1.0 CD A:ARG183 3.9 13.3 1.0 CZ A:ARG183 3.9 28.4 1.0 CA A:GLY180 3.9 8.9 1.0 O A:GLY180 4.4 9.8 1.0 C A:GLY180 4.6 8.4 1.0 CB A:ARG183 4.7 8.3 1.0 CG A:ARG183 4.9 11.0 1.0 N A:GLY180 5.0 10.0 1.0

J.Cuellar, M.Astrand, H.Elovaara, A.Pietikainen, S.Siren, A.Liljeblad, G.Guedez, T.A.Salminen, J.Hytonen. Structural and Biomolecular Analyses Ofborrelia Burgdorferibmpd Reveal A Substrate-Binding Protein of An Abc-Type Nucleoside Transporter Family. Infect.Immun. 2020.
ISSN: ESSN 1098-5522
PubMed: 31988175
DOI: 10.1128/IAI.00962-19