Mercury in PDB 4p1a: Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph

The structure of Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph, PDB code: 4p1a was solved by G.Verdon, O.Boudker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 3.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	106.979, 196.564, 206.499, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 25.7

The structure of Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph also contains other interesting chemical elements:

Thallium

(Tl)

6 atoms

The binding sites of Mercury atom in the Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph (pdb code 4p1a). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph, PDB code: 4p1a:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg503 b:0.5 occ:0.75 SG A:CYS364 2.1 0.6 1.0 SG A:CYS55 2.6 0.4 1.0 CB A:CYS55 2.6 0.8 1.0 CB A:CYS364 3.0 0.1 1.0 CA A:CYS55 3.4 0.5 1.0 NE2 A:HIS368 3.6 0.9 1.0 CD2 A:LEU374 3.8 0.9 1.0 CD1 A:LEU374 3.9 0.3 1.0 CA A:CYS364 4.1 0.8 1.0 OH A:TYR383 4.2 0.2 1.0 N A:CYS55 4.2 0.8 1.0 CD2 A:HIS368 4.3 0.1 1.0 CG A:LEU374 4.3 0.4 1.0 CZ A:TYR383 4.4 0.1 1.0 CE1 A:HIS368 4.4 0.2 1.0 CE2 A:TYR383 4.5 0.8 1.0 C A:CYS55 4.6 0.8 1.0 C A:CYS364 4.7 1.0 1.0 O A:CYS55 4.8 0.4 1.0 O A:CYS364 4.8 0.0 1.0 CB A:LEU374 4.8 0.7 1.0

Mercury binding site 2 out of 3 in the Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg503 b:0.7 occ:0.75 SG B:CYS364 2.1 0.6 1.0 SG B:CYS55 2.7 0.5 1.0 CB B:CYS55 2.9 0.2 1.0 CB B:CYS364 3.0 0.7 1.0 CA B:CYS55 3.5 0.9 1.0 NE2 B:HIS368 3.7 0.6 1.0 CD2 B:LEU374 3.8 0.9 1.0 CA B:CYS364 4.0 0.6 1.0 CD1 B:LEU374 4.1 0.8 1.0 OH B:TYR383 4.2 0.4 1.0 N B:CYS55 4.2 0.5 1.0 CD2 B:HIS368 4.3 0.1 1.0 CZ B:TYR383 4.3 0.2 1.0 CG B:LEU374 4.4 0.4 1.0 CE2 B:TYR383 4.4 0.8 1.0 CE1 B:HIS368 4.6 0.8 1.0 C B:CYS364 4.7 0.2 1.0 C B:CYS55 4.7 0.2 1.0 O B:CYS364 4.9 0.2 1.0 CB B:LEU374 4.9 0.5 1.0 O B:VAL51 5.0 0.5 1.0 CE1 B:TYR383 5.0 0.6 1.0 O B:CYS55 5.0 0.6 1.0

Mercury binding site 3 out of 3 in the Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Thallium-Bound Inward-Facing State of the Glutamate Transporter Homologue Gltph within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg503 b:0.5 occ:0.75 SG C:CYS364 2.2 0.2 1.0 SG C:CYS55 2.6 0.1 1.0 CB C:CYS55 2.7 0.2 1.0 CB C:CYS364 2.9 0.6 1.0 CA C:CYS55 3.4 0.3 1.0 NE2 C:HIS368 3.8 0.9 1.0 CD2 C:LEU374 3.9 0.8 1.0 CA C:CYS364 4.0 1.0 1.0 CD1 C:LEU374 4.1 0.8 1.0 OH C:TYR383 4.1 0.2 1.0 N C:CYS55 4.2 0.6 1.0 CZ C:TYR383 4.3 0.2 1.0 CD2 C:HIS368 4.4 0.2 1.0 CG C:LEU374 4.5 0.8 1.0 CE2 C:TYR383 4.5 0.2 1.0 C C:CYS55 4.6 0.4 1.0 C C:CYS364 4.6 0.4 1.0 CE1 C:HIS368 4.7 0.7 1.0 O C:CYS55 4.8 0.8 1.0 O C:CYS364 4.8 0.1 1.0 O C:VAL51 4.9 0.1 1.0 CE1 C:TYR383 5.0 0.3 1.0 CB C:LEU374 5.0 0.9 1.0

G.Verdon, S.Oh, R.N.Serio, O.Boudker. Coupled Ion Binding and Structural Transitions Along the Transport Cycle of Glutamate Transporters. Elife V. 3 02283 2014.
ISSN: ESSN 2050-084X
PubMed: 24842876
DOI: 10.7554/ELIFE.02283