Chlorine in PDB 2omu: Crystal Structure of Inla G194S+S Y369S/HEC1 Complex

The structure of Crystal Structure of Inla G194S+S Y369S/HEC1 Complex, PDB code: 2omu was solved by T.Wollert, D.W.Heinz, W.D.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	45.010, 54.273, 68.643, 74.98, 80.82, 67.36
R / Rfree (%)	16.4 / 21.7

The structure of Crystal Structure of Inla G194S+S Y369S/HEC1 Complex also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Inla G194S+S Y369S/HEC1 Complex (pdb code 2omu). 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 Inla G194S+S Y369S/HEC1 Complex, PDB code: 2omu:

Chlorine binding site 1 out of 1 in the Crystal Structure of Inla G194S+S Y369S/HEC1 Complex


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 Inla G194S+S Y369S/HEC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1498 b:14.5 occ:0.40 NZ B:LYS25 2.5 18.2 0.6 O A:HOH921 2.7 35.5 1.0 ND2 A:ASN326 2.9 4.2 1.0 O A:HOH512 3.1 8.0 1.0 CE B:LYS25 3.5 18.2 0.6 CD B:LYS25 3.5 16.4 0.6 NZ B:LYS25 3.5 18.5 0.4 CA A:GLY304 3.8 6.1 1.0 CG A:ASN326 3.8 8.2 1.0 OD1 A:ASN326 3.8 10.2 1.0 C A:GLY304 4.0 7.6 1.0 CB A:ALA282 4.0 6.5 1.0 O A:HOH733 4.0 17.4 1.0 O A:GLY304 4.2 7.5 1.0 OE1 A:GLU324 4.3 10.9 1.0 OE2 A:GLU327 4.3 12.3 1.0 OD1 A:ASN283 4.4 16.8 0.5 O B:HOH1529 4.5 29.7 0.6 N A:ALA305 4.5 4.8 1.0 OH A:TYR348 4.5 9.3 1.0 N A:GLY304 4.6 8.1 1.0 CB A:ALA305 4.6 7.2 1.0 CE B:LYS25 4.7 18.3 0.4 O A:HOH1125 4.8 14.5 0.5 CG A:ASN283 4.9 12.4 0.5 ND2 A:ASN283 4.9 11.9 0.5 CG B:LYS25 5.0 17.4 0.6

T.Wollert, D.W.Heinz, W.D.Schubert. Thermodynamically Reengineering the Listerial Invasion Complex Inla/E-Cadherin. Proc.Natl.Acad.Sci.Usa V. 104 13960 2007.
ISSN: ISSN 0027-8424
PubMed: 17715295
DOI: 10.1073/PNAS.0702199104