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Chlorine in PDB 3g3f: Crystal Structure of the GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution

Protein crystallography data

The structure of Crystal Structure of the GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution, PDB code: 3g3f was solved by C.Chaudhry, M.L.Mayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.71 / 1.38
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.185, 114.153, 52.364, 90.00, 115.31, 90.00
R / Rfree (%) 15.2 / 17.5

Other elements in 3g3f:

The structure of Crystal Structure of the GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution also contains other interesting chemical elements:

Sodium (Na) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution (pdb code 3g3f). 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 the GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution, PDB code: 3g3f:

Chlorine binding site 1 out of 1 in 3g3f

Go back to Chlorine Binding Sites List in 3g3f
Chlorine binding site 1 out of 1 in the Crystal Structure of the GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution


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 GLUR6 Ligand Binding Domain Dimer with Glutamate and Nacl at 1.38 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl261

b:15.2
occ:0.84
HZ2 A:LYS104 2.4 18.6 1.0
HZ2 B:LYS104 2.5 20.2 1.0
HH11 B:ARG228 2.6 32.0 0.7
HH11 A:ARG228 2.6 28.6 0.6
O A:HOH386 3.1 26.0 1.0
O B:HOH387 3.1 25.0 1.0
NH1 B:ARG228 3.3 26.6 0.7
NZ A:LYS104 3.3 15.5 1.0
NZ B:LYS104 3.3 16.8 1.0
NH1 A:ARG228 3.3 23.8 0.6
HG3 A:LYS104 3.4 18.0 1.0
HG3 B:LYS104 3.4 17.4 1.0
HH12 B:ARG228 3.4 32.0 0.7
HZ1 B:LYS104 3.4 20.2 1.0
HZ1 A:LYS104 3.4 18.6 1.0
HH12 A:ARG228 3.4 28.6 0.6
HD3 B:ARG228 3.5 20.8 0.7
HD3 A:ARG228 3.6 24.1 0.6
HG2 B:LYS104 3.6 17.4 1.0
HG2 A:LYS104 3.7 18.0 1.0
O A:HOH579 3.7 30.4 0.6
O B:HOH578 3.7 30.1 0.5
HE3 B:LYS104 3.8 20.5 1.0
CZ B:ARG228 3.9 27.3 0.3
HZ3 A:LYS104 3.9 18.6 1.0
CZ A:ARG228 3.9 25.3 0.4
CG B:LYS104 3.9 14.5 1.0
NH2 B:ARG228 3.9 23.7 0.3
HZ3 B:LYS104 4.0 20.2 1.0
CG A:LYS104 4.0 15.0 1.0
HE3 A:LYS104 4.0 20.2 1.0
NE A:ARG228 4.0 19.8 0.4
NH2 A:ARG228 4.0 28.1 0.4
HD3 A:ARG228 4.1 25.4 0.4
HH21 B:ARG228 4.1 28.4 0.3
HG1 B:THR232 4.1 15.6 1.0
NE B:ARG228 4.1 23.7 0.3
CE B:LYS104 4.1 17.1 1.0
HG1 A:THR232 4.1 16.5 1.0
HH21 A:ARG228 4.1 33.7 0.4
CE A:LYS104 4.2 16.9 1.0
HH22 B:ARG228 4.2 28.4 0.3
HD3 B:ARG228 4.2 25.2 0.3
NH1 B:ARG228 4.2 23.9 0.3
O B:PHE102 4.2 11.5 1.0
NH1 A:ARG228 4.2 22.0 0.4
O A:PHE102 4.3 12.4 1.0
HH22 A:ARG228 4.3 33.7 0.4
HE A:ARG228 4.3 23.8 0.4
CD B:ARG228 4.4 17.3 0.7
CD A:ARG228 4.4 20.1 0.6
HE B:ARG228 4.4 28.4 0.3
HD2 A:ARG228 4.4 24.1 0.6
HD2 B:ARG228 4.4 20.8 0.7
HH12 B:ARG228 4.5 28.7 0.3
CZ B:ARG228 4.5 22.8 0.7
HH11 A:ARG228 4.5 26.4 0.4
HH12 A:ARG228 4.5 26.4 0.4
CZ A:ARG228 4.5 22.6 0.6
HH11 B:ARG228 4.5 28.7 0.3
CD A:ARG228 4.6 21.1 0.4
H A:LYS104 4.6 14.0 1.0
H B:LYS104 4.6 13.7 1.0
CD B:LYS104 4.6 16.5 1.0
CD A:LYS104 4.7 15.4 1.0
CD B:ARG228 4.7 21.0 0.3
N B:LYS104 4.8 11.4 1.0
N A:LYS104 4.8 11.7 1.0
O A:HOH567 4.8 15.6 0.6
OD1 A:ASP229 4.8 20.8 1.0
OG1 B:THR232 4.9 13.0 1.0
OG1 A:THR232 4.9 13.8 1.0
NE B:ARG228 4.9 18.7 0.7
O B:HOH454 4.9 12.6 0.5
HG21 A:THR232 4.9 16.4 1.0
OD1 B:ASP229 4.9 21.3 1.0
NE A:ARG228 4.9 18.6 0.6
HE2 B:LYS104 4.9 20.5 1.0
HA B:LYS104 4.9 15.4 1.0
HG21 B:THR232 4.9 15.2 1.0
HG2 A:ARG228 4.9 20.9 0.4
HA A:LYS104 5.0 14.7 1.0
HA B:SER103 5.0 13.8 1.0

Reference:

C.Chaudhry, M.C.Weston, P.Schuck, C.Rosenmund, M.L.Mayer. Stability of Ligand-Binding Domain Dimer Assembly Controls Kainate Receptor Desensitization. Embo J. V. 28 1518 2009.
ISSN: ISSN 0261-4189
PubMed: 19339989
DOI: 10.1038/EMBOJ.2009.86
Page generated: Sat Dec 12 09:43:11 2020

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