Chlorine in PDB 4apx: Crystal Structure of Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I

The structure of Crystal Structure of Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I, PDB code: 4apx was solved by M.Sotomayor, W.Weihofen, R.Gaudet, D.P.Corey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.03 / 1.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	173.606, 40.469, 84.623, 90.00, 103.12, 90.00
R / Rfree (%)	16.138 / 19.307

The structure of Crystal Structure of Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I also contains other interesting chemical elements:

Potassium	(K)	1 atom
Calcium	(Ca)	7 atoms

The binding sites of Chlorine atom in the Crystal Structure of Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I (pdb code 4apx). 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 Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I, PDB code: 4apx:

Chlorine binding site 1 out of 1 in the Crystal Structure of Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I


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 Mouse Cadherin-23 EC1-2 and Protocadherin-15 EC1-2 Form I within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1214 b:54.1 occ:0.50 O A:HOH2302 3.1 34.7 1.0 N A:ILE131 3.6 14.9 1.0 O A:HOH2119 3.8 53.8 1.0 CA A:PHE130 4.1 16.1 1.0 C A:PHE130 4.3 15.3 1.0 CD1 A:PHE130 4.3 19.5 1.0 O A:ILE131 4.3 16.4 1.0 CB A:ILE131 4.4 15.2 1.0 CA A:ILE131 4.5 14.8 1.0 CG A:PHE130 4.5 16.6 1.0 CE1 A:PHE130 4.6 20.3 1.0 CG1 A:ILE131 4.6 15.8 1.0 O A:HOH2303 4.8 34.3 1.0 C A:ILE131 4.9 14.6 1.0 CB A:PHE130 4.9 16.8 1.0 O A:ILE129 5.0 17.5 1.0 CD2 A:PHE130 5.0 16.5 1.0

M.Sotomayor, W.Weihofen, R.Gaudet, D.P.Corey. Structure of A Force-Conveying Cadherin Bond Essential For Inner-Ear Mechanotransduction Nature V. 492 128 2012.
ISSN: ISSN 0028-0836
PubMed: 23135401
DOI: 10.1038/NATURE11590