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Sodium in PDB 7awq: Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101

Protein crystallography data

The structure of Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101, PDB code: 7awq 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) 28.00 / 3.65
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 124, 124, 90.81, 90, 90, 120
R / Rfree (%) 23.3 / 27.1

Other elements in 7awq:

The structure of Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101 also contains other interesting chemical elements:

Barium (Ba) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101 (pdb code 7awq). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101, PDB code: 7awq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 7awq

Go back to Sodium Binding Sites List in 7awq
Sodium binding site 1 out of 2 in the Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na601

b:107.3
occ:1.00
OG1 A:THR130 2.2 92.9 1.0
O A:TYR127 2.2 89.1 1.0
OD1 A:ASN378 2.3 94.9 1.0
OG1 A:THR131 2.6 84.8 1.0
OD1 A:ASP380 2.8 100.7 1.0
C A:TYR127 3.0 89.6 1.0
CA A:TYR127 3.1 81.8 1.0
CG A:ASN378 3.3 97.2 1.0
N A:THR131 3.3 90.9 1.0
CB A:THR130 3.4 99.0 1.0
CB A:THR131 3.7 90.3 1.0
C A:THR130 3.8 97.8 1.0
CG A:ASP380 3.9 98.1 1.0
O A:TYR126 3.9 97.2 1.0
CA A:THR130 3.9 96.6 1.0
CA A:THR131 4.0 88.1 1.0
CB A:TYR127 4.0 77.5 1.0
ND2 A:ASN378 4.1 89.4 1.0
CB A:ASN378 4.1 67.8 1.0
N A:THR130 4.2 99.1 1.0
N A:TYR127 4.2 86.8 1.0
OD2 A:ASP380 4.3 103.5 1.0
CA A:ASN378 4.3 64.2 1.0
N A:MET128 4.3 90.2 1.0
CD1 A:TYR127 4.4 75.8 1.0
C A:TYR126 4.5 95.7 1.0
O A:THR130 4.6 99.0 1.0
CG2 A:THR130 4.6 101.6 1.0
CG A:TYR127 4.7 74.9 1.0
C A:ASN378 4.9 67.7 1.0
CG2 A:THR131 5.0 86.8 1.0

Sodium binding site 2 out of 2 in 7awq

Go back to Sodium Binding Sites List in 7awq
Sodium binding site 2 out of 2 in the Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of the Thermostabilized EAAT1 Cryst-E386Q Mutant in Complex with L-Asp, Sodium Ions and the Allosteric Inhibitor UCPH101 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na602

b:41.9
occ:1.00
O A:THR376 2.2 48.4 1.0
CE A:MET379 2.3 55.2 1.0
O A:ALA420 2.3 49.3 1.0
O A:SER417 2.8 58.0 1.0
SD A:MET379 2.9 63.2 1.0
C A:THR376 3.0 48.4 1.0
C A:ALA420 3.4 48.7 1.0
CG A:MET379 3.5 63.1 1.0
O A:ILE418 3.5 53.4 1.0
N A:ILE377 3.7 47.8 1.0
CA A:THR376 3.9 41.2 1.0
CA A:ILE377 3.9 52.2 1.0
O A:ILE377 3.9 64.9 1.0
C A:ILE418 3.9 57.5 1.0
C A:SER417 3.9 62.2 1.0
CA A:ALA420 4.1 47.9 1.0
N A:ALA420 4.1 50.5 1.0
C A:ILE377 4.1 61.8 1.0
CB A:MET379 4.2 64.5 1.0
CA A:ILE418 4.3 57.2 1.0
C A:GLY419 4.3 52.2 1.0
CB A:ALA420 4.4 51.9 1.0
N A:ALA421 4.5 41.2 1.0
O A:GLY419 4.5 48.0 1.0
OG1 A:THR376 4.5 50.1 1.0
N A:ILE418 4.6 60.1 1.0
N A:GLY419 4.6 55.5 1.0
CA A:ALA421 4.8 37.1 1.0
C A:ALA421 4.8 41.6 1.0
O A:ALA375 4.8 43.5 1.0
CB A:THR376 4.9 48.2 1.0
N A:THR376 4.9 42.2 1.0

Reference:

J.Canul-Tec, J.Dhenin, R.Assal, P.Legrand, R.Martial, J.Chamot-Rooke, N.Reyes. Ion-Coupling Mechanism of Excitatory Amino Acid Transporters To Be Published.
Page generated: Fri Nov 5 16:02:17 2021

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