Chlorine in PDB 3dlp: 4-Chlorobenzoyl-Coa Ligase/Synthetase, Mutant D402P, Bound to 4CB

All present enzymatic activity of 4-Chlorobenzoyl-Coa Ligase/Synthetase, Mutant D402P, Bound to 4CB:
6.2.1.33;

The structure of 4-Chlorobenzoyl-Coa Ligase/Synthetase, Mutant D402P, Bound to 4CB, PDB code: 3dlp was solved by R.Wu, J.Cao, A.S.Reger, X.Lu, A.M.Gulick, D.Dunaway-Mariano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	127.922, 127.922, 71.230, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 25.2

The binding sites of Chlorine atom in the 4-Chlorobenzoyl-Coa Ligase/Synthetase, Mutant D402P, Bound to 4CB (pdb code 3dlp). 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 4-Chlorobenzoyl-Coa Ligase/Synthetase, Mutant D402P, Bound to 4CB, PDB code: 3dlp:

Chlorine binding site 1 out of 1 in the 4-Chlorobenzoyl-Coa Ligase/Synthetase, Mutant D402P, Bound to 4CB


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, Mutant D402P, Bound to 4CB within 5.0Å range: probe atom residue distance (Å) B Occ X:Cl909 b:62.7 occ:1.00 CL4 X:174909 0.0 62.7 1.0 C4 X:174909 1.8 62.9 1.0 C5 X:174909 2.7 62.9 1.0 C3 X:174909 2.8 61.8 1.0 CZ X:PHE184 3.6 44.4 1.0 CG2 X:ILE303 3.7 50.4 1.0 N X:ASN311 3.7 45.8 1.0 CA X:ASN311 3.7 44.9 1.0 C X:MET310 3.8 48.6 1.0 CB X:ASN311 3.8 44.6 1.0 CG X:MET310 3.9 49.4 1.0 CE1 X:PHE184 3.9 44.8 1.0 O X:MET310 3.9 52.6 1.0 C6 X:174909 4.0 62.4 1.0 CA X:GLY305 4.1 46.8 1.0 CE X:MET310 4.1 48.2 1.0 C2 X:174909 4.1 62.3 1.0 CE2 X:PHE184 4.2 44.2 1.0 CG2 X:VAL209 4.2 43.2 1.0 SD X:MET310 4.3 49.4 1.0 CA X:MET310 4.3 49.4 1.0 OD1 X:ASN311 4.4 50.0 1.0 CG X:ASN311 4.5 45.7 1.0 N X:GLY305 4.5 47.4 1.0 C1 X:174909 4.6 63.0 1.0 O X:TYR304 4.6 49.0 1.0 CB X:MET310 4.7 49.4 1.0 C X:TYR304 4.8 48.0 1.0 CD1 X:PHE184 4.8 42.8 1.0 C X:GLY305 4.9 48.1 1.0

R.Wu, A.S.Reger, X.Lu, A.M.Gulick, D.Dunaway-Mariano. The Mechanism of Domain Alternation in the Acyl-Adenylate Forming Ligase Superfamily Member 4-Chlorobenzoate: Coenzyme A Ligase Biochemistry V. 48 4115 2009.
ISSN: ISSN 0006-2960
PubMed: 19320426
DOI: 10.1021/BI9002327