Chlorine in PDB 4ojj: X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator)

The structure of X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator), PDB code: 4ojj was solved by Z.Fourati-Kammoun, O.Kolesnikova, R.Back, J.Keller, N.Lazar, C.Gaudon-Plesse, B.Seraphin, M.Graille, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.86 / 2.32
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	36.430, 173.540, 175.440, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 29.3

The structure of X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator) also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Chlorine atom in the X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator) (pdb code 4ojj). 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 X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator), PDB code: 4ojj:

Chlorine binding site 1 out of 1 in the X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of the C-Terminal Domain of PAT1 (Decapping Activator) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl903 b:72.6 occ:1.00 CZ2 C:TRP508 3.9 47.5 1.0 CG C:GLN547 4.0 45.4 1.0 CE2 C:TRP508 4.2 45.0 1.0 NE1 C:TRP508 4.4 48.8 1.0 CA C:GLN547 4.5 46.0 1.0 CH2 C:TRP508 4.6 48.2 1.0 N C:GLN547 4.7 52.7 1.0 O C:GLN546 4.7 46.2 1.0 C C:GLN546 4.8 50.4 1.0 CB C:GLN547 4.8 47.0 1.0 CB C:GLN546 5.0 52.1 1.0

Z.Fourati, O.Kolesnikova, R.Back, J.Keller, C.Charenton, V.Taverniti, C.G.Plesse, N.Lazar, D.Durand, H.Van Tilbeurgh, B.Seraphin, M.Graille. The C-Terminal Domain From S. Cerevisiae PAT1 Displays Two Conserved Regions Involved in Decapping Factor Recruitment. Plos One V. 9 96828 2014.
ISSN: ESSN 1932-6203
PubMed: 24830408
DOI: 10.1371/JOURNAL.PONE.0096828