Chlorine in PDB 3trg: Structure of An Acylphosphatase From Coxiella Burnetii

All present enzymatic activity of Structure of An Acylphosphatase From Coxiella Burnetii:
3.6.1.7;

The structure of Structure of An Acylphosphatase From Coxiella Burnetii, PDB code: 3trg was solved by J.Cheung, M.C.Franklin, M.Rudolph, M.Cassidy, E.Gary, F.Burshteyn, J.Love, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.30 / 1.60
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	69.710, 69.710, 40.059, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 18.9

The binding sites of Chlorine atom in the Structure of An Acylphosphatase From Coxiella Burnetii (pdb code 3trg). 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 Structure of An Acylphosphatase From Coxiella Burnetii, PDB code: 3trg:

Chlorine binding site 1 out of 1 in the Structure of An Acylphosphatase From Coxiella Burnetii


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of An Acylphosphatase From Coxiella Burnetii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl96 b:18.2 occ:0.73 NH1 A:ARG29 3.0 13.9 1.0 O A:HOH242 3.0 22.5 1.0 N A:VAL94 3.2 10.0 1.0 CA A:ARG93 3.5 10.1 1.0 CD A:ARG29 3.5 8.0 1.0 CG2 A:VAL94 3.7 16.2 1.0 C A:ARG93 3.8 10.3 1.0 CB A:ARG93 4.0 13.0 1.0 CZ A:ARG29 4.0 13.7 1.0 O A:HOH141 4.2 23.9 0.9 O A:PHE92 4.2 11.3 1.0 NE A:ARG29 4.2 13.0 1.0 CA A:VAL94 4.2 10.8 1.0 CB A:VAL94 4.3 12.2 1.0 CG A:ARG93 4.3 15.8 1.0 CG1 A:VAL94 4.3 9.2 1.0 O A:VAL94 4.5 14.0 1.0 N A:ARG93 4.7 8.5 1.0 CG A:ARG29 4.8 9.0 1.0 C A:PHE92 4.9 9.9 1.0 C A:VAL94 4.9 11.7 1.0

M.C.Franklin, J.Cheung, M.J.Rudolph, F.Burshteyn, M.Cassidy, E.Gary, B.Hillerich, Z.K.Yao, P.R.Carlier, M.Totrov, J.D.Love. Structural Genomics For Drug Design Against the Pathogen Coxiella Burnetii. Proteins V. 83 2124 2015.
ISSN: ISSN 0887-3585
PubMed: 26033498
DOI: 10.1002/PROT.24841