Chlorine in PDB 5cmk: Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195

The structure of Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195, PDB code: 5cmk was solved by S.Chittori, M.L.Mayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.86 / 1.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.759, 102.759, 281.992, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 18.7

The structure of Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195 also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195 (pdb code 5cmk). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195, PDB code: 5cmk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195


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 the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:18.7 occ:0.83 HZ2 A:LYS104 2.3 17.5 1.0 HZ2 B:LYS104 2.3 19.3 1.0 O B:HOH468 2.9 31.2 1.0 O A:HOH434 3.0 29.5 1.0 NZ A:LYS104 3.1 14.6 1.0 NZ B:LYS104 3.2 16.1 1.0 HG3 A:LYS104 3.3 20.5 1.0 HG3 B:LYS104 3.3 20.5 1.0 HZ1 A:LYS104 3.3 17.5 1.0 HZ1 B:LYS104 3.3 19.3 1.0 HG2 A:LYS104 3.5 20.5 1.0 HZ3 A:LYS104 3.5 17.5 1.0 HG2 B:LYS104 3.5 20.5 1.0 HZ3 B:LYS104 3.6 19.3 1.0 HH11 A:ARG228 3.6 51.1 1.0 CG A:LYS104 3.8 17.1 1.0 HD3 A:ARG228 3.8 40.8 1.0 NH1 A:ARG228 3.9 42.6 1.0 CG B:LYS104 3.9 17.1 1.0 HH11 B:ARG228 3.9 50.0 1.0 HD3 B:ARG228 3.9 39.8 1.0 HG1 A:THR232 3.9 16.1 1.0 NH1 B:ARG228 3.9 41.6 1.0 HE3 B:LYS104 4.0 19.9 1.0 HG1 B:THR232 4.0 17.6 1.0 HH12 A:ARG228 4.0 51.1 1.0 O A:PHE102 4.1 13.2 1.0 CE B:LYS104 4.1 16.6 1.0 HH12 B:ARG228 4.1 50.0 1.0 CE A:LYS104 4.2 15.9 1.0 O B:PHE102 4.2 12.1 1.0 HE3 A:LYS104 4.2 19.1 1.0 CZ B:ARG228 4.3 41.1 1.0 CZ A:ARG228 4.4 40.5 1.0 H A:LYS104 4.5 13.9 1.0 HA A:LYS104 4.5 16.1 1.0 H B:LYS104 4.6 14.6 1.0 N A:LYS104 4.6 11.6 1.0 NE B:ARG228 4.6 40.6 1.0 CD A:ARG228 4.6 34.0 1.0 HA B:LYS104 4.6 16.4 1.0 CD B:LYS104 4.6 17.6 1.0 CD B:ARG228 4.6 33.2 1.0 CD A:LYS104 4.6 17.0 1.0 N B:LYS104 4.6 12.2 1.0 HG21 B:THR232 4.7 18.2 1.0 OG1 A:THR232 4.7 13.4 1.0 NE A:ARG228 4.7 40.3 1.0 HD2 A:ARG228 4.8 40.8 1.0 OG1 B:THR232 4.8 14.6 1.0 C A:SER103 4.8 11.5 1.0 HA A:SER103 4.8 15.2 1.0 HD2 B:ARG228 4.8 39.8 1.0 HG21 A:THR232 4.8 14.9 1.0 NH2 B:ARG228 4.9 39.4 1.0 HA B:SER103 4.9 15.6 1.0 CA A:LYS104 4.9 13.5 1.0 HE2 B:LYS104 4.9 19.9 1.0 C B:SER103 5.0 12.5 1.0 HE2 A:LYS104 5.0 19.1 1.0 CA B:LYS104 5.0 13.6 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the GLUK2EM Lbd Dimer Assembly Complex with Glutamate and LY466195 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl305 b:50.9 occ:0.87 HA B:ARG4 3.0 34.4 1.0 OD1 B:ASN3 3.4 75.9 1.0 O B:HOH699 3.5 46.6 1.0 HB2 B:ARG4 3.6 37.8 1.0 CA B:ARG4 3.8 28.6 1.0 N B:ARG4 4.0 29.3 1.0 CB B:ARG4 4.1 31.5 1.0 HG3 B:ARG4 4.1 39.3 1.0 H B:ARG4 4.2 35.2 1.0 CG B:ASN3 4.5 74.0 1.0 C B:ASN3 4.5 33.3 1.0 O B:ASN3 4.6 26.7 1.0 CG B:ARG4 4.6 32.8 1.0 H B:SER5 4.7 25.3 1.0 HD21 B:ASN3 4.9 99.7 1.0 HB3 B:ARG4 5.0 37.8 1.0

J.R.Meyerson, S.Chittori, A.Merk, P.Rao, T.H.Han, M.Serpe, M.L.Mayer, S.Subramaniam. Structural Basis of Kainate Subtype Glutamate Receptor Desensitization. Nature V. 537 567 2016.
ISSN: ESSN 1476-4687
PubMed: 27580033
DOI: 10.1038/NATURE19352