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Mercury in PDB 4p19: Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph

Protein crystallography data

The structure of Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph, PDB code: 4p19 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 / 3.25
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 109.933, 201.812, 207.142, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 25.8

Mercury Binding Sites:

The binding sites of Mercury atom in the Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph (pdb code 4p19). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph, PDB code: 4p19:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in 4p19

Go back to Mercury Binding Sites List in 4p19
Mercury binding site 1 out of 3 in the Closed, Apo 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 Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg501

b:0.2
occ:0.75
SG A:CYS364 2.5 0.4 1.0
SG A:CYS55 2.5 0.8 1.0
CB A:CYS55 2.7 0.2 1.0
CB A:CYS364 3.0 91.6 1.0
CA A:CYS55 3.3 98.0 1.0
CD2 A:LEU374 3.6 0.3 1.0
CD1 A:LEU374 3.9 0.8 1.0
OH A:TYR383 4.0 0.1 1.0
N A:CYS55 4.0 93.0 1.0
CZ A:TYR383 4.2 0.6 1.0
CA A:CYS364 4.2 89.9 1.0
NE2 A:HIS368 4.3 0.7 1.0
CE2 A:TYR383 4.3 99.6 1.0
CG A:LEU374 4.3 0.1 1.0
C A:CYS55 4.6 90.2 1.0
CD2 A:HIS368 4.8 0.1 1.0
CE1 A:TYR383 4.8 95.8 1.0
O A:CYS55 4.8 87.6 1.0
O A:VAL51 4.9 80.4 1.0
CB A:LEU374 5.0 0.7 1.0

Mercury binding site 2 out of 3 in 4p19

Go back to Mercury Binding Sites List in 4p19
Mercury binding site 2 out of 3 in the Closed, Apo 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 Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg501

b:0.5
occ:0.75
SG B:CYS364 2.2 0.5 1.0
SG B:CYS55 2.4 0.1 1.0
CB B:CYS55 2.8 0.1 1.0
CB B:CYS364 3.0 97.0 1.0
CD2 B:LEU374 3.4 96.8 1.0
CA B:CYS55 3.4 0.5 1.0
CD1 B:LEU374 3.7 95.0 1.0
NE2 B:HIS368 3.9 0.6 1.0
N B:CYS55 4.0 0.1 1.0
CG B:LEU374 4.1 0.7 1.0
CA B:CYS364 4.2 89.7 1.0
OH B:TYR383 4.2 96.7 1.0
CE2 B:TYR383 4.2 85.4 1.0
CZ B:TYR383 4.4 89.2 1.0
CD2 B:HIS368 4.5 0.4 1.0
O B:VAL51 4.6 75.8 1.0
C B:CYS55 4.7 91.9 1.0
CB B:LEU374 4.8 0.2 1.0
CG1 B:VAL51 4.8 55.9 1.0
CE1 B:HIS368 4.9 0.2 1.0
C B:CYS364 5.0 89.6 1.0
O B:CYS55 5.0 95.6 1.0
CD2 B:TYR383 5.0 86.1 1.0

Mercury binding site 3 out of 3 in 4p19

Go back to Mercury Binding Sites List in 4p19
Mercury binding site 3 out of 3 in the Closed, Apo 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 Closed, Apo Inward-Facing State of the Glutamate Transporter Homologue Gltph within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Hg501

b:0.3
occ:0.75
SG C:CYS364 2.5 0.1 1.0
SG C:CYS55 2.8 0.1 1.0
CB C:CYS364 3.0 85.0 1.0
CB C:CYS55 3.1 0.2 1.0
CA C:CYS55 3.5 0.3 1.0
CD2 C:LEU374 3.6 0.7 1.0
CD1 C:LEU374 3.8 0.9 1.0
OH C:TYR383 3.9 0.1 1.0
CZ C:TYR383 4.1 0.4 1.0
CE2 C:TYR383 4.1 0.8 1.0
CA C:CYS364 4.1 86.1 1.0
NE2 C:HIS368 4.1 0.1 1.0
CG C:LEU374 4.3 0.7 1.0
N C:CYS55 4.3 88.8 1.0
C C:CYS55 4.7 97.0 1.0
O C:CYS55 4.8 94.1 1.0
CE1 C:HIS368 4.8 0.8 1.0
CD2 C:HIS368 4.9 0.7 1.0
CE1 C:TYR383 4.9 0.4 1.0
CD2 C:TYR383 4.9 0.9 1.0
CG1 C:VAL58 4.9 89.3 1.0

Reference:

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
Page generated: Sun Dec 13 19:11:34 2020

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