Chlorine in PDB 6ulu: D104A/S128A S. Typhimurium Siroheme Synthase

All present enzymatic activity of D104A/S128A S. Typhimurium Siroheme Synthase:
1.3.1.76; 2.1.1.107; 4.99.1.4;

The structure of D104A/S128A S. Typhimurium Siroheme Synthase, PDB code: 6ulu was solved by J.M.Pennington, M.E.Stroupe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.17 / 2.76
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.940, 99.913, 147.545, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 28.5

The binding sites of Chlorine atom in the D104A/S128A S. Typhimurium Siroheme Synthase (pdb code 6ulu). 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 D104A/S128A S. Typhimurium Siroheme Synthase, PDB code: 6ulu:

Chlorine binding site 1 out of 1 in the D104A/S128A S. Typhimurium Siroheme Synthase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of D104A/S128A S. Typhimurium Siroheme Synthase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:98.6 occ:1.00 N B:GLY130 2.9 54.2 1.0 N B:ALA128 3.2 24.4 1.0 C B:ALA128 3.3 42.2 1.0 N B:GLY129 3.4 49.1 1.0 N B:SER132 3.4 35.5 1.0 CA B:GLY130 3.5 48.0 1.0 CA B:ALA128 3.5 36.8 1.0 N B:THR131 3.6 48.5 1.0 CB B:ALA128 3.6 41.3 1.0 C B:GLY130 3.7 52.1 1.0 N B:PRO133 3.8 49.4 1.0 C B:SER132 3.8 47.5 1.0 O B:ALA128 3.8 26.3 1.0 C B:GLY129 4.0 54.7 1.0 OG B:SER127 4.0 41.8 1.0 O B:SER132 4.1 50.8 1.0 CA B:SER132 4.2 37.6 1.0 CD B:PRO133 4.2 33.9 1.0 CA B:PRO133 4.2 54.7 1.0 CA B:GLY129 4.2 48.5 1.0 C B:THR131 4.4 47.2 1.0 O B:GLY130 4.4 27.9 1.0 C B:SER127 4.4 36.1 1.0 OG1 B:THR131 4.5 47.3 1.0 CA B:THR131 4.5 51.1 1.0 OG B:SER132 4.6 49.9 1.0 CA B:SER127 4.8 35.8 1.0 CB B:PRO133 4.8 39.9 1.0 CB B:SER132 4.9 41.9 1.0

J.M.Pennington, M.Kemp, L.Mcgarry, Y.Chen, M.E.Stroupe. Siroheme Synthase Orients Substrates For Dehydrogenase and Chelatase Activities in A Common Active Site. Nat Commun V. 11 864 2020.
ISSN: ESSN 2041-1723
PubMed: 32054833
DOI: 10.1038/S41467-020-14722-1