Chlorine in PDB 8c4o: Cdaa-Atp Complex

All present enzymatic activity of Cdaa-Atp Complex:
2.7.7.85;

The structure of Cdaa-Atp Complex, PDB code: 8c4o was solved by P.Neumann, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.73 / 1.97
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.5, 64.65, 129.39, 90, 90, 90
R / Rfree (%)	23.5 / 25.4

The structure of Cdaa-Atp Complex also contains other interesting chemical elements:

Manganese	(Mn)	3 atoms
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the Cdaa-Atp Complex (pdb code 8c4o). 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 Cdaa-Atp Complex, PDB code: 8c4o:

Chlorine binding site 1 out of 1 in the Cdaa-Atp Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cdaa-Atp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl202 b:79.1 occ:1.00 HG B:SER56 2.6 69.1 1.0 OG B:SER56 3.1 57.5 1.0 HD12 B:ILE60 3.3 63.6 1.0 HG3 B:GLN57 3.3 66.4 1.0 HB2 B:SER56 3.4 64.3 1.0 HD11 B:ILE60 3.6 63.6 1.0 HZ2 B:LYS18 3.6 105.7 1.0 CD1 B:ILE60 3.8 53.0 1.0 CB B:SER56 3.8 53.5 1.0 HD13 B:ILE60 4.0 63.6 1.0 HB3 B:LYS18 4.0 73.7 1.0 HA B:GLN57 4.1 62.2 1.0 CG B:GLN57 4.2 55.3 1.0 CD B:GLN57 4.3 56.4 1.0 HZ1 B:LYS18 4.3 105.7 1.0 NZ B:LYS18 4.4 88.1 1.0 N B:GLN57 4.4 52.0 1.0 C B:SER56 4.5 52.7 1.0 NE2 B:GLN57 4.5 65.2 1.0 HB3 B:SER56 4.5 64.3 1.0 HE21 B:GLN57 4.5 78.3 1.0 H B:GLN57 4.6 62.4 1.0 HG3 A:PRO68 4.7 73.8 1.0 HZ3 B:LYS18 4.7 105.7 1.0 CA B:GLN57 4.7 51.8 1.0 HB3 A:PRO68 4.7 78.5 1.0 OE1 B:GLN57 4.7 54.7 1.0 HG2 B:GLN57 4.7 66.4 1.0 HG2 B:LYS18 4.8 90.5 1.0 O B:SER56 4.8 52.3 1.0 CA B:SER56 4.8 51.7 1.0 HE22 B:GLN57 4.9 78.3 1.0 CB B:LYS18 5.0 61.4 1.0

P.Neumann, P.Kloskowski, R.Ficner. Computer-Aided Design of A Cyclic Di-Amp Synthesizing Enzyme Cdaa Inhibitor. Microlife V. 4 AD021 2023.
ISSN: ISSN 2633-6693
PubMed: 37223749
DOI: 10.1093/FEMSML/UQAD021