Chlorine in PDB 6g8k: 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide

The structure of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide, PDB code: 6g8k was solved by S.A.Andrei, V.Thijssen, L.Brunsveld, C.Ottmann, L.G.Milroy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.87 / 1.25
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.260, 111.730, 62.510, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 16

The structure of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Sodium	(Na)	1 atom

The binding sites of Chlorine atom in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide (pdb code 6g8k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide, PDB code: 6g8k:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:13.9 occ:1.00 O A:HOH729 3.0 23.4 1.0 HD2 A:LYS87 3.0 22.1 0.4 HA A:TYR84 3.1 12.4 1.0 O A:HOH670 3.1 18.9 1.0 HD2 A:LYS87 3.2 21.4 0.6 HD1 A:TYR84 3.2 13.1 1.0 HB2 A:LYS87 3.4 16.8 0.4 HB2 A:LYS87 3.4 16.2 0.6 HB3 A:GLU83 3.6 12.9 1.0 HD3 A:LYS87 3.7 21.4 0.6 HB2 A:TYR84 3.8 12.4 1.0 CD A:LYS87 3.8 18.4 0.4 CD A:LYS87 3.8 17.8 0.6 CA A:TYR84 3.8 10.4 1.0 HD3 A:LYS87 3.8 22.1 0.4 O A:GLU83 3.9 10.5 1.0 HB3 A:LYS87 3.9 16.2 0.6 HB3 A:LYS87 4.0 16.8 0.4 N A:TYR84 4.0 10.0 1.0 CB A:LYS87 4.1 13.5 0.6 CB A:LYS87 4.1 14.0 0.4 CD1 A:TYR84 4.1 10.9 1.0 C A:GLU83 4.1 10.3 1.0 CB A:TYR84 4.2 10.3 1.0 CB A:GLU83 4.3 10.7 1.0 HB2 A:GLU83 4.4 12.9 1.0 HZ3 A:LYS87 4.4 26.3 0.4 CG A:LYS87 4.5 16.3 0.4 H A:TYR84 4.5 12.0 1.0 CG A:LYS87 4.5 15.6 0.6 O A:HOH511 4.5 19.2 1.0 CG A:TYR84 4.6 10.3 1.0 HG3 A:LYS87 4.7 19.5 0.4 HZ1 A:LYS87 4.8 26.3 0.4 HG3 A:LYS87 4.8 18.8 0.6 CA A:GLU83 4.9 10.6 1.0 H A:LYS87 4.9 14.4 0.6 H A:LYS87 4.9 14.4 0.4 NZ A:LYS87 4.9 21.9 0.4 O A:HOH749 4.9 41.0 1.0 CE A:LYS87 4.9 20.5 0.4

Chlorine binding site 2 out of 2 in the 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of 14-3-3SIGMA in Complex with A S131BETA3S Mutated Yap PS127 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:14.1 occ:0.47 HH12 A:ARG148 2.0 11.5 0.5 HG A:SER186 2.1 15.3 1.0 HD1 A:HIS180 2.2 12.8 1.0 NH1 A:ARG148 2.8 9.6 0.5 O A:HOH722 2.8 19.8 1.0 ND1 A:HIS180 2.8 10.7 1.0 OG A:SER186 2.9 12.8 1.0 HB2 A:SER186 3.0 14.6 1.0 HH11 A:ARG148 3.1 11.5 0.5 HB1 A:ALA184 3.1 15.9 1.0 HE1 A:HIS180 3.2 13.1 1.0 CB A:SER186 3.3 12.2 1.0 HB3 A:ALA184 3.3 15.9 1.0 CE1 A:HIS180 3.3 10.9 1.0 HB3 A:SER186 3.4 14.6 1.0 HH22 A:ARG148 3.6 17.1 0.5 CB A:ALA184 3.6 13.3 1.0 HG2 A:GLU189 3.7 12.7 1.0 CZ A:ARG148 3.9 12.5 0.5 HA A:HIS180 4.0 11.4 1.0 CG A:HIS180 4.0 10.1 1.0 HB2 A:ALA184 4.0 15.9 1.0 HB3 A:GLU189 4.1 12.0 1.0 NH2 A:ARG148 4.1 14.2 0.5 O A:HOH599 4.1 17.2 1.0 HE2 A:PHE179 4.2 13.1 1.0 HB3 A:HIS180 4.3 11.8 1.0 O A:HOH503 4.5 15.5 1.0 O A:HOH709 4.5 34.9 1.0 HB2 A:GLU189 4.5 12.0 1.0 CG A:GLU189 4.5 10.6 1.0 CB A:HIS180 4.5 9.9 1.0 NE2 A:HIS180 4.6 10.9 1.0 CB A:GLU189 4.6 10.0 1.0 O A:ALA184 4.7 14.0 1.0 O A:HOH645 4.7 44.9 1.0 CA A:HIS180 4.7 9.5 1.0 CA A:SER186 4.8 11.3 1.0 CD2 A:HIS180 4.9 10.5 1.0 CE2 A:PHE179 4.9 10.9 1.0 HH21 A:ARG148 5.0 17.1 0.5 CA A:ALA184 5.0 12.5 1.0

S.A.Andrei, V.Thijssen, L.Brunsveld, C.Ottmann, L.G.Milroy. A Study on the Effect of Synthetic Alpha-to-BETA3-Amino Acid Mutations on the Binding of Phosphopeptides to 14-3-3 Proteins. Chem.Commun.(Camb.) 2019.
ISSN: ESSN 1364-548X
PubMed: 31763628
DOI: 10.1039/C9CC07982C