Chlorine in PDB 5weo: Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin

The binding sites of Chlorine atom in the Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin (pdb code 5weo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin, PDB code: 5weo:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1302 b:0.5 occ:1.00 CL A:CYZ1302 0.0 0.5 1.0 C13 A:CYZ1302 1.7 0.5 1.0 C14 A:CYZ1302 2.7 0.5 1.0 C12 A:CYZ1302 2.7 0.5 1.0 O4 A:CYZ1302 3.1 0.5 1.0 S2 A:CYZ1302 3.2 0.5 1.0 OD1 A:ASP760 3.2 0.1 1.0 N3 A:CYZ1302 3.5 0.5 1.0 OG D:SER729 3.8 0.8 1.0 C11 A:CYZ1302 4.0 0.5 1.0 CB D:SER729 4.0 0.8 1.0 C10 A:CYZ1302 4.0 0.5 1.0 O A:PHE495 4.1 0.7 1.0 CG A:ASP760 4.3 0.1 1.0 C9 A:CYZ1302 4.4 0.5 1.0 O3 A:CYZ1302 4.6 0.5 1.0 OD2 A:ASP760 4.6 0.1 1.0 CB A:LEU759 4.9 0.4 1.0

Chlorine binding site 2 out of 4 in the Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1302 b:0.4 occ:1.00 CL B:CYZ1302 0.0 0.4 1.0 C13 B:CYZ1302 1.7 0.4 1.0 C12 B:CYZ1302 2.7 0.4 1.0 C14 B:CYZ1302 2.7 0.4 1.0 OD1 B:ASP760 3.1 0.0 1.0 S2 B:CYZ1302 3.1 0.4 1.0 O4 B:CYZ1302 3.2 0.4 1.0 N3 B:CYZ1302 3.2 0.4 1.0 C11 B:CYZ1302 4.0 0.4 1.0 C10 B:CYZ1302 4.0 0.4 1.0 CG B:ASP760 4.0 0.0 1.0 OG C:SER729 4.0 0.6 1.0 CB C:SER729 4.2 0.6 1.0 O B:PHE495 4.2 0.2 1.0 OD2 B:ASP760 4.3 0.0 1.0 C9 B:CYZ1302 4.4 0.4 1.0 CB B:LEU759 4.5 0.6 1.0 O3 B:CYZ1302 4.5 0.4 1.0 CD1 B:LEU759 4.7 0.6 1.0

Chlorine binding site 3 out of 4 in the Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1302 b:0.2 occ:1.00 CL C:CYZ1302 0.0 0.2 1.0 C13 C:CYZ1302 1.7 0.2 1.0 C14 C:CYZ1302 2.7 0.2 1.0 C12 C:CYZ1302 2.7 0.2 1.0 O4 C:CYZ1302 3.1 0.2 1.0 OD1 C:ASP760 3.1 0.5 1.0 S2 C:CYZ1302 3.2 0.2 1.0 N3 C:CYZ1302 3.7 0.2 1.0 OG B:SER729 3.9 0.3 1.0 C11 C:CYZ1302 4.0 0.2 1.0 C10 C:CYZ1302 4.0 0.2 1.0 O C:PHE495 4.1 0.0 1.0 CB B:SER729 4.2 0.3 1.0 CG C:ASP760 4.2 0.5 1.0 C9 C:CYZ1302 4.4 0.2 1.0 O3 C:CYZ1302 4.6 0.2 1.0 OD2 C:ASP760 4.7 0.5 1.0 NZ C:LYS763 4.9 0.3 1.0 CB C:LEU759 4.9 0.1 1.0

Chlorine binding site 4 out of 4 in the Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Activated GLUA2 Complex Bound to Glutamate, Cyclothiazide, and Stz in Digitonin within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl1302 b:0.9 occ:1.00 CL D:CYZ1302 0.0 0.9 1.0 C13 D:CYZ1302 1.7 0.9 1.0 C12 D:CYZ1302 2.7 0.9 1.0 C14 D:CYZ1302 2.7 0.9 1.0 OD1 D:ASP760 3.1 0.7 1.0 S2 D:CYZ1302 3.1 0.9 1.0 O4 D:CYZ1302 3.2 0.9 1.0 N3 D:CYZ1302 3.2 0.9 1.0 OG A:SER729 3.9 0.5 1.0 C11 D:CYZ1302 4.0 0.9 1.0 C10 D:CYZ1302 4.0 0.9 1.0 CB A:SER729 4.0 0.5 1.0 CG D:ASP760 4.1 0.7 1.0 O D:PHE495 4.2 0.6 1.0 OD2 D:ASP760 4.4 0.7 1.0 C9 D:CYZ1302 4.4 0.9 1.0 O3 D:CYZ1302 4.5 0.9 1.0 CB D:LEU759 4.7 0.1 1.0 CD1 D:LEU759 4.8 0.1 1.0

E.C.Twomey, M.V.Yelshanskaya, R.A.Grassucci, J.Frank, A.I.Sobolevsky. Channel Opening and Gating Mechanism in Ampa-Subtype Glutamate Receptors. Nature V. 549 60 2017.
ISSN: ISSN 0028-0836
PubMed: 28737760
DOI: 10.1038/NATURE23479