Chlorine in PDB 4qpj: 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain

The structure of 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain, PDB code: 4qpj was solved by J.W.Willett, J.Herrou, S.Crosson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.88 / 2.74
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	124.951, 124.951, 136.332, 90.00, 90.00, 120.00
R / Rfree (%)	17.5 / 22.2

The structure of 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Calcium	(Ca)	3 atoms
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain (pdb code 4qpj). 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 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain, PDB code: 4qpj:

Chlorine binding site 1 out of 1 in the 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 2.7 Angstrom Structure of A Phosphotransferase in Complex with A Receiver Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:81.4 occ:1.00 OE1 B:GLN180 2.9 52.9 1.0 NH2 B:ARG19 3.3 52.8 1.0 NH1 B:ARG19 3.9 59.2 1.0 CD B:PRO181 4.0 43.5 1.0 CD B:GLN180 4.0 55.7 1.0 CZ B:ARG19 4.0 62.2 1.0 CB B:GLN180 4.3 50.7 1.0 CG B:GLN180 4.5 49.8 1.0 O B:HIS177 4.6 57.8 1.0 O B:LEU121 4.7 53.1 1.0 CD1 B:ILE122 4.8 50.0 1.0 CG B:PRO181 4.9 49.3 1.0

J.W.Willett, J.Herrou, A.Briegel, G.Rotskoff, S.Crosson. Structural Asymmetry in A Conserved Signaling System That Regulates Division, Replication, and Virulence of An Intracellular Pathogen. Proc.Natl.Acad.Sci.Usa V. 112 E3709 2015.
ISSN: ISSN 0027-8424
PubMed: 26124143
DOI: 10.1073/PNAS.1503118112