Chlorine in PDB 6r89: Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine

Protein crystallography data

The structure of Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine, PDB code: 6r89 was solved by A.Alfieri, R.Pederzoli, A.Costa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.40 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 97.661, 98.544, 114.154, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 22.8

Other elements in 6r89:

The structure of Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine (pdb code 6r89). 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 Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine, PDB code: 6r89:

Chlorine binding site 1 out of 1 in 6r89

Go back to Chlorine Binding Sites List in 6r89
Chlorine binding site 1 out of 1 in the Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Arabidopsis Thaliana GLR3.3 Ligand-Binding Domain in Complex with L-Cysteine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl303

b:62.6
occ:1.00
CE C:LYS236 4.1 63.7 1.0
O C:LYS236 4.3 36.6 1.0
CG C:LYS236 4.6 53.9 1.0
CH2 C:TRP237 4.9 38.6 1.0
CZ3 C:TRP237 4.9 40.6 1.0

Reference:

A.Alfieri, F.G.Doccula, R.Pederzoli, M.Grenzi, M.C.Bonza, L.Luoni, A.Candeo, N.Romano Armada, A.Barbiroli, G.Valentini, T.R.Schneider, A.Bassi, M.Bolognesi, M.Nardini, A.Costa. The Structural Bases For Agonist Diversity in An Arabidopsis Thaliana Glutamate Receptor-Like Channel Proc.Natl.Acad.Sci.Usa 2019.
ISSN: ESSN 1091-6490
DOI: 10.1073/PNAS.1905142117
Page generated: Sat Dec 12 13:35:48 2020

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