Chlorine in PDB 3cw9: 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa

All present enzymatic activity of 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa:
6.2.1.33;

The structure of 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa, PDB code: 3cw9 was solved by A.S.Reger, J.Cao, R.Wu, D.Dunaway-Mariano, A.M.Gulick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.507, 87.789, 186.060, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 20.9

The structure of 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa (pdb code 3cw9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa, PDB code: 3cw9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl990 b:17.8 occ:1.00 CL4A A:01A990 0.0 17.8 1.0 C4 A:01A990 1.8 18.4 1.0 C5 A:01A990 2.7 17.7 1.0 C3 A:01A990 2.8 17.4 1.0 N A:ASN311 3.5 14.8 1.0 CG2 A:ILE303 3.6 14.2 1.0 C A:MET310 3.7 14.7 1.0 CA A:ASN311 3.7 14.9 1.0 CZ A:PHE184 3.8 14.0 1.0 CB A:ASN311 3.8 15.2 1.0 CG A:MET310 4.0 14.9 1.0 C6 A:01A990 4.0 18.0 1.0 C2 A:01A990 4.1 18.3 1.0 CA A:GLY305 4.1 14.3 1.0 CE A:MET310 4.1 14.3 1.0 O A:MET310 4.1 14.7 1.0 CE1 A:PHE184 4.1 12.3 1.0 CA A:MET310 4.2 14.3 1.0 SD A:MET310 4.3 15.2 1.0 CE2 A:PHE184 4.4 13.5 1.0 C1' A:01A990 4.6 18.6 1.0 O A:TYR304 4.6 14.0 1.0 N A:GLY305 4.6 14.2 1.0 CB A:MET310 4.6 14.5 1.0 OD1 A:ASN311 4.6 20.0 1.0 CG A:ASN311 4.7 16.9 1.0 CG2 A:VAL209 4.7 13.9 1.0 C A:TYR304 4.8 13.9 1.0 C A:GLY305 4.9 14.8 1.0 CD1 A:PHE184 5.0 12.2 1.0

Chlorine binding site 2 out of 2 in the 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 4-Chlorobenzoyl-Coa Ligase/Synthetase in the Thioester-Forming Conformation, Bound to 4-Chlorophenacyl-Coa within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl991 b:15.5 occ:1.00 CL4A B:01A991 0.0 15.5 1.0 C4 B:01A991 1.8 15.6 1.0 C5 B:01A991 2.7 15.3 1.0 C3 B:01A991 2.8 14.4 1.0 N B:ASN311 3.5 14.3 1.0 CG2 B:ILE303 3.6 13.6 1.0 CZ B:PHE184 3.7 13.9 1.0 CA B:ASN311 3.7 14.9 1.0 C B:MET310 3.7 13.9 1.0 CB B:ASN311 3.9 15.1 1.0 CG B:MET310 3.9 12.9 1.0 CE B:MET310 4.0 14.2 1.0 C6 B:01A991 4.0 15.2 1.0 C2 B:01A991 4.1 14.8 1.0 CE1 B:PHE184 4.1 13.4 1.0 O B:MET310 4.2 13.8 1.0 SD B:MET310 4.2 14.4 1.0 CA B:MET310 4.2 13.4 1.0 CE2 B:PHE184 4.2 14.0 1.0 CA B:GLY305 4.3 13.2 1.0 OD1 B:ASN311 4.6 20.9 1.0 C1' B:01A991 4.6 15.4 1.0 CG2 B:VAL209 4.6 12.5 1.0 CB B:MET310 4.6 13.5 1.0 CG B:ASN311 4.7 17.6 1.0 O B:TYR304 4.7 13.8 1.0 N B:GLY305 4.8 13.6 1.0 CD1 B:PHE184 5.0 13.7 1.0 C B:GLY305 5.0 13.5 1.0 C B:TYR304 5.0 13.3 1.0

A.S.Reger, R.Wu, D.Dunaway-Mariano, A.M.Gulick. Structural Characterization of A 140 Degrees Domain Movement in the Two-Step Reaction Catalyzed By 4-Chlorobenzoate:Coa Ligase. Biochemistry V. 47 8016 2008.
ISSN: ISSN 0006-2960
PubMed: 18620418
DOI: 10.1021/BI800696Y