Fluorine in PDB 5mju: Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101

The structure of Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101, PDB code: 5mju was solved by J.Canul-Tec, R.Assal, P.Legrand, N.Reyes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 3.71
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	124.330, 124.330, 90.810, 90.00, 90.00, 120.00
R / Rfree (%)	22.7 / 25.4

The binding sites of Fluorine atom in the Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101 (pdb code 5mju). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101, PDB code: 5mju:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101 within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:0.6 occ:1.00 F2 A:7O9602 0.0 0.6 1.0 C13 A:7O9602 1.3 0.3 1.0 F A:7O9602 2.1 0.6 1.0 F1 A:7O9602 2.1 0.1 1.0 C12 A:7O9602 2.4 0.2 1.0 C14 A:7O9602 3.1 0.9 1.0 O A:PRO372 3.1 38.0 1.0 C11 A:7O9602 3.4 0.4 1.0 CG2 A:ILE100 3.6 71.0 1.0 CG2 A:ILE223 3.6 72.2 1.0 CG2 A:THR376 3.7 64.5 1.0 OG1 A:THR376 3.8 72.4 1.0 C A:PRO372 4.1 38.6 1.0 CD2 A:LEU349 4.1 49.0 1.0 CB A:ALA375 4.2 47.8 1.0 CB A:THR376 4.3 68.2 1.0 CA A:PRO372 4.3 32.5 1.0 C15 A:7O9602 4.4 0.5 1.0 N A:THR376 4.6 57.6 1.0 C10 A:7O9602 4.6 0.1 1.0 CB A:ILE100 4.8 68.2 1.0 CB A:PRO372 4.8 33.5 1.0 CB A:ILE223 4.9 71.3 1.0 C A:ALA375 4.9 58.2 1.0 CA A:THR376 4.9 59.9 1.0

Fluorine binding site 2 out of 3 in the Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101 within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:0.6 occ:1.00 F A:7O9602 0.0 0.6 1.0 C13 A:7O9602 1.3 0.3 1.0 F1 A:7O9602 2.1 0.1 1.0 F2 A:7O9602 2.1 0.6 1.0 C12 A:7O9602 2.4 0.2 1.0 C11 A:7O9602 2.7 0.4 1.0 CG2 A:ILE223 3.2 72.2 1.0 CD1 A:ILE96 3.3 78.4 1.0 CG2 A:ILE100 3.4 71.0 1.0 C14 A:7O9602 3.6 0.9 1.0 OG A:SER346 4.0 65.6 1.0 C10 A:7O9602 4.1 0.1 1.0 CD1 A:ILE223 4.2 74.3 1.0 CB A:ILE96 4.4 61.8 1.0 CG1 A:ILE96 4.4 61.6 1.0 CB A:ILE223 4.4 71.3 1.0 CG1 A:ILE223 4.5 70.2 1.0 CG1 A:ILE100 4.5 66.2 1.0 CB A:ILE100 4.5 68.2 1.0 CD1 A:ILE100 4.6 78.6 1.0 CD2 A:LEU349 4.7 49.0 1.0 CB A:SER346 4.7 56.1 1.0 C15 A:7O9602 4.8 0.5 1.0 CA A:SER346 4.8 52.8 1.0 CG2 A:THR376 4.8 64.5 1.0 C9 A:7O9602 5.0 0.7 1.0

Fluorine binding site 3 out of 3 in the Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of the Thermostabilized EAAT1 Cryst Mutant in Complex with the Competititve Inhibitor Tfb-Tboa and the Allosteric Inhibitor UCPH101 within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:0.1 occ:1.00 F1 A:7O9602 0.0 0.1 1.0 C13 A:7O9602 1.3 0.3 1.0 F A:7O9602 2.1 0.6 1.0 F2 A:7O9602 2.1 0.6 1.0 C12 A:7O9602 2.3 0.2 1.0 C14 A:7O9602 2.9 0.9 1.0 CD2 A:LEU349 3.2 49.0 1.0 C11 A:7O9602 3.5 0.4 1.0 CA A:SER346 3.7 52.8 1.0 CB A:LEU349 3.8 40.7 1.0 CG A:LEU349 4.0 48.1 1.0 CG2 A:ILE100 4.0 71.0 1.0 OG A:SER346 4.0 65.6 1.0 CB A:ALA375 4.1 47.8 1.0 CB A:SER346 4.2 56.1 1.0 C15 A:7O9602 4.2 0.5 1.0 O A:SER346 4.2 51.7 1.0 C A:SER346 4.5 54.2 1.0 O A:SER345 4.5 62.2 1.0 N A:SER346 4.6 56.5 1.0 C10 A:7O9602 4.6 0.1 1.0 CD1 A:LEU349 4.6 51.3 1.0 O A:PRO372 4.6 38.0 1.0 CD1 A:ILE96 4.7 78.4 1.0 CB A:ILE96 4.7 61.8 1.0 CG2 A:ILE96 4.9 63.3 1.0 C A:SER345 4.9 63.2 1.0 C9 A:7O9602 4.9 0.7 1.0

J.C.Canul-Tec, R.Assal, E.Cirri, P.Legrand, S.Brier, J.Chamot-Rooke, N.Reyes. Structure and Allosteric Inhibition of Excitatory Amino Acid Transporter 1. Nature V. 544 446 2017.
ISSN: ESSN 1476-4687
PubMed: 28424515
DOI: 10.1038/NATURE22064