Chlorine in PDB 2xvs: Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain

The structure of Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain, PDB code: 2xvs was solved by J.Adams, A.C.W.Pike, S.Maniam, T.D.Sharpe, A.S.Coutts, S.Knapp, B.La Thangue, A.N.Bullock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.77 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	30.260, 62.390, 78.770, 90.00, 90.00, 90.00
R / Rfree (%)	17.242 / 23.638

The structure of Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain also contains other interesting chemical elements:

Iodine

(I)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain (pdb code 2xvs). 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 Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain, PDB code: 2xvs:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human TTC5 (Strap) C-Terminal Ob Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1427 b:55.4 occ:1.00 OG A:SER344 3.3 10.4 1.0 N A:LEU345 3.9 9.3 1.0 CE2 A:PHE353 4.0 18.8 1.0 CB A:SER344 4.0 10.3 1.0 CA A:LEU345 4.0 9.0 1.0 C A:SER344 4.0 12.8 1.0 CZ A:PHE353 4.3 16.7 1.0 C A:LEU345 4.3 9.4 1.0 O A:SER344 4.3 13.6 1.0 CD2 A:PHE353 4.6 16.9 1.0 CA A:SER344 4.7 12.2 1.0 N A:THR346 4.7 10.7 1.0 O A:LEU345 4.7 10.4 1.0 O A:HOH2046 4.8 33.6 1.0 O A:HOH2050 4.8 17.1 1.0

C.J.Adams, A.C.Pike, S.Maniam, T.D.Sharpe, A.S.Coutts, S.Knapp, N.B.La Thangue, A.N.Bullock. The P53 Cofactor Strap Exhibits An Unexpected Tpr Motif and Oligonucleotide-Binding (Ob)-Fold Structure. Proc.Natl.Acad.Sci.Usa V. 109 3778 2012.
ISSN: ISSN 0027-8424
PubMed: 22362889
DOI: 10.1073/PNAS.1113731109