Chlorine in PDB 6qdt: Crystal Structure of 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide

The structure of Crystal Structure of 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide, PDB code: 6qdt was solved by S.A.Andrei, A.Kaplan, A.E.Fournier, C.Ottman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.87 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.657, 112.411, 62.749, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 19.2

The structure of Crystal Structure of 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide also contains other interesting chemical elements:

Calcium	(Ca)	1 atom
Sodium	(Na)	5 atoms

The binding sites of Chlorine atom in the Crystal Structure of 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide (pdb code 6qdt). 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 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide, PDB code: 6qdt:

Chlorine binding site 1 out of 1 in the Crystal Structure of 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide


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 14-3-3SIGMA in Complex with A RAPGEF2 PT740 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:13.4 occ:1.00 HZ1 A:LYS9 2.3 12.0 1.0 HD3 A:LYS9 3.0 11.0 1.0 NZ A:LYS9 3.2 10.0 1.0 HZ3 A:LYS9 3.4 12.0 1.0 HZ A:PHE25 3.5 12.4 1.0 HZ2 A:LYS9 3.7 12.0 1.0 CD A:LYS9 3.8 9.1 1.0 HE3 A:MET1 3.9 17.6 1.0 CE A:LYS9 3.9 9.6 1.0 HE2 A:LYS9 4.0 11.6 1.0 HE2 A:PHE25 4.0 11.6 1.0 HD2 A:LYS9 4.1 11.0 1.0 CZ A:PHE25 4.3 10.3 1.0 HE1 A:MET1 4.4 17.6 1.0 CE2 A:PHE25 4.5 9.7 1.0 CE A:MET1 4.6 14.6 1.0 HE3 A:LYS9 4.8 11.6 1.0 O A:HOH757 4.9 38.6 1.0

A.Kaplan, S.A.Andrei, C.Ottmann, A.E.Fournier. A Single-Agent Polypharmacological Approach to Stimulate Axon Regeneration To Be Published.