Barium in PDB 7awl: Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101

The structure of Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101, PDB code: 7awl was solved by J.C.Canul-Tec, P.Legrand, N.Reyes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.00 / 3.70
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	124.94, 124.94, 92.02, 90, 90, 120
R / Rfree (%)	23.7 / 28.5

The binding sites of Barium atom in the Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101 (pdb code 7awl). This binding sites where shown within 5.0 Angstroms radius around Barium atom.
In total 2 binding sites of Barium where determined in the Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101, PDB code: 7awl:
Jump to Barium binding site number: 1; 2;

Barium binding site 1 out of 2 in the Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 1 of Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba602 b:186.0 occ:0.35 OE1 A:GLN245 3.9 170.4 1.0

Barium binding site 2 out of 2 in the Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Barium with other atoms in the Ba binding site number 2 of Structure of the Thermostabilized EAAT1 Cryst-II Mutant in Complex with Barium and the Allosteric Inhibitor UCPH101 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ba603 b:149.9 occ:0.60 OD1 A:ASP380 2.6 154.8 1.0 O A:TYR127 2.7 152.1 1.0 OD1 A:ASN378 2.8 156.2 1.0 OG1 A:THR131 2.8 165.5 1.0 CA A:TYR127 3.3 139.2 1.0 C A:TYR127 3.4 151.8 1.0 OG1 A:THR130 3.4 157.4 1.0 CG A:ASP380 3.5 152.4 1.0 CG A:ASN378 3.7 155.8 1.0 CB A:TYR127 3.7 133.6 1.0 OD2 A:ASP380 3.8 156.8 1.0 CD1 A:TYR127 3.8 127.2 1.0 N A:MET379 3.8 128.3 1.0 CB A:THR131 4.1 167.4 1.0 CA A:ASN378 4.1 121.5 1.0 CG A:TYR127 4.3 127.9 1.0 N A:THR131 4.3 161.2 1.0 N A:ASP380 4.3 138.3 1.0 CB A:ASN378 4.5 122.2 1.0 C A:ASN378 4.5 127.8 1.0 ND2 A:ASN378 4.6 148.5 1.0 N A:TYR127 4.6 142.6 1.0 CB A:THR130 4.6 163.6 1.0 CA A:THR131 4.6 161.1 1.0 O A:TYR126 4.6 153.5 1.0 N A:MET128 4.6 155.8 1.0 CB A:ASP380 4.8 144.6 1.0 CA A:MET379 4.8 131.8 1.0 O A:ILE377 4.8 126.8 1.0 C A:THR130 4.8 167.2 1.0 CE1 A:TYR127 4.9 122.5 1.0

J.Canul-Tec, A.Kumar, J.Dhenin, R.Assal, P.Legrand, R.Martial, J.Chamott-Rooke, N.Reyes. Ion-Coupling Mechanism of Excitatory Amino Acid Transporters To Be Published.