Chlorine in PDB 6au1: Structure of the Pgab (Bpsb) Glycoside Hydrolase Domain From Bordetella Bronchiseptica

The structure of Structure of the Pgab (Bpsb) Glycoside Hydrolase Domain From Bordetella Bronchiseptica, PDB code: 6au1 was solved by D.J.Little, N.C.Bamford, P.L.Howell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.83 / 1.76
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.102, 91.649, 75.295, 90.00, 111.51, 90.00
R / Rfree (%)	15.1 / 16.7

The binding sites of Chlorine atom in the Structure of the Pgab (Bpsb) Glycoside Hydrolase Domain From Bordetella Bronchiseptica (pdb code 6au1). 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 Structure of the Pgab (Bpsb) Glycoside Hydrolase Domain From Bordetella Bronchiseptica, PDB code: 6au1:

Chlorine binding site 1 out of 1 in the Structure of the Pgab (Bpsb) Glycoside Hydrolase Domain From Bordetella Bronchiseptica


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Pgab (Bpsb) Glycoside Hydrolase Domain From Bordetella Bronchiseptica within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl705 b:19.9 occ:1.00 O B:HOH973 3.1 20.5 1.0 NE1 B:TRP393 3.1 16.0 1.0 NE B:ARG390 3.2 20.7 1.0 ND2 B:ASN389 3.6 17.6 1.0 NH2 B:ARG390 3.7 24.1 1.0 CZ B:ARG390 3.9 23.1 1.0 CD1 B:TRP393 4.1 15.1 1.0 CE2 B:TRP393 4.1 16.8 1.0 CD B:ARG390 4.1 19.5 1.0 CZ2 B:TRP393 4.4 18.0 1.0 CA B:ARG390 4.5 14.1 1.0 CB B:ARG390 4.5 16.1 1.0 CG B:ASN389 4.7 16.7 1.0 N B:ARG390 4.8 14.0 1.0 CG B:ARG390 4.9 17.8 1.0

D.J.Little, R.Pfoh, F.Le Mauff, N.C.Bamford, C.Notte, P.Baker, M.Guragain, H.Robinson, G.B.Pier, M.Nitz, R.Deora, D.C.Sheppard, P.L.Howell. Pgab Orthologues Contain A Glycoside Hydrolase Domain That Cleaves Deacetylated Poly-Beta (1,6)-N-Acetylglucosamine and Can Disrupt Bacterial Biofilms. Plos Pathog. V. 14 06998 2018.
ISSN: ESSN 1553-7374
PubMed: 29684093
DOI: 10.1371/JOURNAL.PPAT.1006998