Chlorine in PDB 3hrk: Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex)

All present enzymatic activity of Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex):
6.1.1.21;

The structure of Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex), PDB code: 3hrk was solved by T.L.Arakaki, E.A.Merritt, E.T.Larson, Medical Structural Genomics Ofpathogenic Protozoa (Msgpp), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.56 / 3.05
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	112.360, 166.987, 66.021, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 30.8

The binding sites of Chlorine atom in the Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex) (pdb code 3hrk). 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 Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex), PDB code: 3hrk:

Chlorine binding site 1 out of 1 in the Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Histidyl-Trna Synthetase From Trypanosoma Cruzi (Histidyl-Adenylate Complex) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl3 b:47.0 occ:1.00 NH2 A:ARG69 3.0 37.1 1.0 NH2 B:ARG69 3.0 37.2 1.0 NH1 B:ARG69 3.6 35.8 1.0 CZ B:ARG69 3.7 35.1 1.0 CZ A:ARG69 3.8 36.4 1.0 NH1 A:ARG69 3.8 37.5 1.0 NE2 B:HIS76 4.5 7.8 1.0 NE2 A:HIS76 4.8 19.1 1.0 NE B:ARG69 4.9 32.0 1.0 NE A:ARG69 5.0 33.7 1.0

E.A.Merritt, T.L.Arakaki, J.R.Gillespie, E.T.Larson, A.Kelley, N.Mueller, A.J.Napuli, J.Kim, L.Zhang, C.L.Verlinde, E.Fan, F.Zucker, F.S.Buckner, W.C.Van Voorhis, W.G.Hol. Crystal Structures of Trypanosomal Histidyl-Trna Synthetase Illuminate Differences Between Eukaryotic and Prokaryotic Homologs. J.Mol.Biol. V. 397 481 2010.
ISSN: ISSN 0022-2836
PubMed: 20132829
DOI: 10.1016/J.JMB.2010.01.051