Table 1

Table 1. Glt_pH residues identified in our computations to play a functional role and their EAAT1 counterparts
Glt_ph residue	Structural element	Role inferred from MD *(rows 9-10)* and ENM *(rows 11-12)*	EAAT1 counterpart
G354, G357	HP2	Glu recognition, loop flexibility	G442, Q445
S277-S279	HP1	Glu binding (3-Ser motif)	S364-S366
D312-T314	TM7	Glu coordination (NMDGT motif)	*D400-T402*
R397-T398	TM8	Stabilization of bound glutamate	*R479-T480*
T314	TM7	Water binding	T402
N401, V400	TM8	Water binding	*N483, T482*
D390, D394	TM8	Pathway for water and Na+ ions entry/exit and Glu stabilization	D472, D476
N310, A307, D312	TM7	Na⁺ binding site I	N398, A395 *D400*
N401, G404	TM8	Na⁺ binding site I	*N483, G486*
L303, G306	TM7	Na⁺ binding site II	L391,G394
D405	TM8	Na⁺ binding site II	D487
M286	HP1	Blockers on exit pathway – (delivery to the IC region)	F373
L303	TM7	Blockers on exit pathway – (delivery to the IC region)	L391
G144	TM4	Hinge center for global opening/closing of the trimer	E184
L183	TM5	Hinge center for global opening/closing of the trimer	R268
H114 H332	L34 TM7/8 loop	Potential sites for capture of anions from the EC region	K152 E420

Residues implicated in recognition and binding of glutamate, water or Na+ ions, as seen in the simulation analysis. The equivalent residues in EAAT1 are given in the fourth column. Residues highlighted in bold are those which are highly conserved, bold & underlined are those which are both conserved and implicated in the function of transport and/or binding.