Chlorine in PDB 6bwl: X-Ray Structure of Pal From Bacillus Thuringiensis

All present enzymatic activity of X-Ray Structure of Pal From Bacillus Thuringiensis:
4.2.1.46;

The structure of X-Ray Structure of Pal From Bacillus Thuringiensis, PDB code: 6bwl was solved by N.A.Delvaux, J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.50 / 1.45
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	96.420, 98.341, 98.603, 90.00, 90.00, 90.00
R / Rfree (%)	12.9 / 15.1

The structure of X-Ray Structure of Pal From Bacillus Thuringiensis also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Chlorine atom in the X-Ray Structure of Pal From Bacillus Thuringiensis (pdb code 6bwl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the X-Ray Structure of Pal From Bacillus Thuringiensis, PDB code: 6bwl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the X-Ray Structure of Pal From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of Pal From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:25.7 occ:1.00 OG A:SER249 3.2 13.1 1.0 ND2 A:ASN251 3.4 12.1 1.0 O A:HOH893 3.5 39.9 1.0 O A:HOH972 3.6 40.7 1.0 CB A:SER249 3.6 12.7 1.0 CB A:ASN251 3.8 11.2 1.0 O A:HOH888 4.0 39.5 1.0 CG A:ASN251 4.1 12.3 1.0 O A:HOH602 4.2 21.4 1.0 CG A:LYS211 4.4 15.8 1.0 CA A:LYS211 4.4 11.4 1.0 O A:GLY210 4.5 10.9 1.0 O A:HOH934 4.6 30.5 1.0 CG A:LYS252 4.7 17.7 1.0 CB A:LYS211 4.8 14.0 1.0 NZ A:LYS252 5.0 48.9 1.0 CA A:ASN251 5.0 10.8 1.0 N A:LYS252 5.0 10.8 1.0

Chlorine binding site 2 out of 2 in the X-Ray Structure of Pal From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Structure of Pal From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl408 b:24.9 occ:1.00 OH A:TYR147 2.8 11.7 1.0 OG1 A:THR122 3.0 12.8 1.0 O A:HOH800 3.0 35.2 1.0 O A:HOH513 3.2 32.8 1.0 CE1 A:TYR147 3.6 9.9 1.0 C4N A:NAD401 3.6 11.6 1.0 CZ A:TYR147 3.6 9.2 1.0 C3N A:NAD401 3.7 9.1 1.0 C5N A:NAD401 3.8 13.5 1.0 CB A:THR122 3.8 11.2 1.0 C2N A:NAD401 3.8 9.2 1.0 N1N A:NAD401 3.9 10.1 1.0 C6N A:NAD401 3.9 12.3 1.0 CG A:MET124 4.0 13.3 1.0 C7N A:NAD401 4.3 10.9 1.0 O7N A:NAD401 4.5 10.9 1.0 O A:HOH796 4.5 46.3 1.0 O2D A:NAD401 4.5 9.6 1.0 CG2 A:THR122 4.6 11.3 1.0 O2B A:UDP402 4.6 24.7 1.0 C1D A:NAD401 4.8 9.4 1.0 C2D A:NAD401 4.9 8.4 1.0 CA A:THR122 4.9 9.3 1.0 CE2 A:TYR147 4.9 8.5 1.0 CD1 A:TYR147 4.9 9.3 1.0 O A:ILE83 4.9 15.4 1.0

N.A.Delvaux, J.B.Thoden, H.M.Holden. Molecular Architectures of Pen and Pal: Key Enzymes Required For Cmp-Pseudaminic Acid Biosynthesis in Bacillus Thuringiensis. Protein Sci. V. 27 738 2018.
ISSN: ESSN 1469-896X
PubMed: 29266550
DOI: 10.1002/PRO.3368