Mercury in PDB 6x15: Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions

The structure of Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions also contains other interesting chemical elements:

Sodium

(Na)

9 atoms

The binding sites of Mercury atom in the Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions (pdb code 6x15). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions, PDB code: 6x15:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg505 b:54.4 occ:0.30 OH A:TYR383 2.5 37.8 1.0 SG A:CYS364 2.8 37.8 1.0 CZ A:TYR383 3.3 37.8 1.0 SG A:CYS55 3.3 34.4 1.0 CE2 A:TYR383 3.4 37.8 1.0 CB A:LEU54 3.5 32.7 1.0 C A:LEU54 3.6 32.7 1.0 N A:CYS55 3.7 34.4 1.0 O A:LEU54 3.7 32.7 1.0 O A:ALA360 3.8 33.7 1.0 CA A:CYS55 3.9 34.4 1.0 CA A:LEU54 4.2 32.7 1.0 CB A:CYS55 4.3 34.4 1.0 CA A:ILE361 4.3 33.3 1.0 CE1 A:TYR383 4.4 37.8 1.0 O A:VAL51 4.4 33.6 1.0 CB A:CYS364 4.5 37.8 1.0 O A:ILE361 4.6 33.3 1.0 C A:ALA360 4.7 33.7 1.0 CD2 A:TYR383 4.7 37.8 1.0 CD1 A:LEU54 4.7 32.7 1.0 CG A:LEU54 4.7 32.7 1.0 CD2 A:LEU374 4.8 45.0 1.0 CG2 A:VAL58 4.9 30.7 1.0 N A:ILE361 4.9 33.3 1.0 C A:ILE361 5.0 33.3 1.0

Mercury binding site 2 out of 3 in the Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg506 b:54.4 occ:0.30 OH B:TYR383 2.5 37.8 1.0 SG B:CYS364 2.8 37.8 1.0 CZ B:TYR383 3.3 37.8 1.0 SG B:CYS55 3.3 34.4 1.0 CE2 B:TYR383 3.4 37.8 1.0 CB B:LEU54 3.5 32.7 1.0 C B:LEU54 3.6 32.7 1.0 N B:CYS55 3.7 34.4 1.0 O B:LEU54 3.7 32.7 1.0 O B:ALA360 3.8 33.7 1.0 CA B:CYS55 3.9 34.4 1.0 CA B:LEU54 4.2 32.7 1.0 CB B:CYS55 4.3 34.4 1.0 CA B:ILE361 4.3 33.3 1.0 CE1 B:TYR383 4.4 37.8 1.0 O B:VAL51 4.4 33.6 1.0 CB B:CYS364 4.5 37.8 1.0 O B:ILE361 4.6 33.3 1.0 C B:ALA360 4.7 33.7 1.0 CD2 B:TYR383 4.7 37.8 1.0 CD1 B:LEU54 4.7 32.7 1.0 CG B:LEU54 4.7 32.7 1.0 CD2 B:LEU374 4.8 45.0 1.0 CG2 B:VAL58 4.9 30.7 1.0 N B:ILE361 4.9 33.3 1.0 C B:ILE361 5.0 33.3 1.0

Mercury binding site 3 out of 3 in the Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Inward-Facing State of the Glutamate Transporter Homologue Gltph in Complex with L-Aspartate and Sodium Ions within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg506 b:54.4 occ:0.30 OH C:TYR383 2.5 37.8 1.0 SG C:CYS364 2.8 37.8 1.0 CZ C:TYR383 3.3 37.8 1.0 SG C:CYS55 3.3 34.4 1.0 CE2 C:TYR383 3.4 37.8 1.0 CB C:LEU54 3.5 32.7 1.0 C C:LEU54 3.6 32.7 1.0 N C:CYS55 3.7 34.4 1.0 O C:LEU54 3.7 32.7 1.0 O C:ALA360 3.8 33.7 1.0 CA C:CYS55 3.9 34.4 1.0 CA C:LEU54 4.2 32.7 1.0 CB C:CYS55 4.3 34.4 1.0 CA C:ILE361 4.3 33.3 1.0 CE1 C:TYR383 4.4 37.8 1.0 O C:VAL51 4.4 33.6 1.0 CB C:CYS364 4.5 37.8 1.0 O C:ILE361 4.6 33.3 1.0 C C:ALA360 4.7 33.7 1.0 CD2 C:TYR383 4.7 37.8 1.0 CD1 C:LEU54 4.7 32.7 1.0 CG C:LEU54 4.7 32.7 1.0 CD2 C:LEU374 4.8 45.0 1.0 CG2 C:VAL58 4.9 30.7 1.0 N C:ILE361 4.9 33.3 1.0 C C:ILE361 5.0 33.3 1.0

X.Wang, O.Boudker. Large Domain Movements Through the Lipid Bilayer Mediate Substrate Release and Inhibition of Glutamate Transporters. Elife V. 9 2020.
ISSN: ESSN 2050-084X
PubMed: 33155546
DOI: 10.7554/ELIFE.58417