Sodium in PDB 4uxu: Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine

The structure of Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine, PDB code: 4uxu was solved by M.Zouridakis, P.Giastas, E.Zarkadas, S.J.Tzartos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.606 / 1.71
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.434, 66.246, 75.191, 90.00, 102.76, 90.00
R / Rfree (%)	20.6 / 23.46

The binding sites of Sodium atom in the Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine (pdb code 4uxu). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine, PDB code: 4uxu:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1218 b:32.7 occ:1.00 O A:HOH3263 2.1 43.1 1.0 O B:GLY193 2.4 20.8 1.0 ND2 A:ASN162 2.8 17.3 1.0 O B:SER191 2.9 19.8 1.0 N A:LYS187 3.0 16.1 1.0 N B:GLY193 3.4 20.7 1.0 C A:VAL186 3.4 19.2 1.0 CB A:LYS187 3.4 19.1 1.0 C B:GLY193 3.4 21.1 1.0 O A:HOH3192 3.4 24.2 1.0 C B:SER191 3.6 19.4 1.0 CA A:VAL186 3.7 18.6 1.0 C B:TYR192 3.7 24.5 1.0 OG B:SER191 3.7 34.9 1.0 CA A:LYS187 3.8 17.2 1.0 CG A:ASN162 3.8 17.6 1.0 CA B:GLY193 3.9 21.1 1.0 CB A:ASN162 4.0 16.9 1.0 CA B:TYR192 4.1 20.2 1.0 N B:TYR192 4.1 19.8 1.0 O A:VAL186 4.1 15.6 1.0 O A:ALA185 4.2 15.2 1.0 O B:TYR192 4.3 20.8 1.0 O B:HOH3211 4.4 51.0 1.0 N A:VAL186 4.4 14.3 1.0 O B:HOH3212 4.4 41.0 1.0 CB B:SER191 4.5 26.7 1.0 C A:ALA185 4.6 14.4 1.0 N B:CYS194 4.6 21.5 1.0 CA B:SER191 4.6 19.5 1.0 N A:ASN162 4.8 16.0 1.0 CG A:LYS187 4.8 16.4 1.0 CB A:VAL186 4.9 21.7 1.0 OD1 A:ASN162 5.0 18.5 1.0

Sodium binding site 2 out of 2 in the Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of the Extracellular Domain of the Human ALPHA9 Nicotinic Acetylcholine Receptor in Complex with Methyllycaconitine within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1217 b:27.9 occ:1.00 O A:HOH3234 2.3 46.9 1.0 O A:GLY193 2.6 21.1 1.0 ND2 B:ASN162 2.8 17.6 1.0 O A:SER191 3.0 18.9 1.0 N B:LYS187 3.1 16.9 1.0 O B:HOH3184 3.1 21.7 1.0 CB B:LYS187 3.3 17.5 1.0 C B:VAL186 3.4 16.9 1.0 N A:GLY193 3.6 21.0 1.0 OG A:SER191 3.6 33.2 1.0 C A:GLY193 3.6 21.7 1.0 C A:SER191 3.6 20.7 1.0 CA B:VAL186 3.7 17.7 1.0 CA B:LYS187 3.7 17.3 1.0 CG B:ASN162 3.8 20.4 1.0 C A:TYR192 3.8 24.5 1.0 CB B:ASN162 3.9 18.6 1.0 CA A:GLY193 4.0 22.6 1.0 O B:VAL186 4.1 17.2 1.0 N A:TYR192 4.1 19.3 1.0 O A:HOH3242 4.2 45.8 1.0 CA A:TYR192 4.2 19.9 1.0 O A:HOH3236 4.3 47.0 1.0 O A:TYR192 4.3 20.8 1.0 O B:ALA185 4.4 17.1 1.0 CB A:SER191 4.4 25.2 1.0 N B:VAL186 4.5 16.9 1.0 CA A:SER191 4.6 21.3 1.0 C B:ALA185 4.7 17.6 1.0 CG B:LYS187 4.7 17.2 1.0 N B:ASN162 4.8 17.7 1.0 N A:CYS194 4.8 25.0 1.0 CB B:VAL186 4.9 24.0 1.0 C B:LYS187 5.0 17.4 1.0 OD1 B:ASN162 5.0 18.1 1.0

M.Zouridakis, P.Giastas, E.Zarkadas, D.Chroni-Tzartou, P.Bregestovski, S.J.Tzartos. Crystal Structures of Free and Antagonist-Bound States of Human ALPHA9 Nicotinic Receptor Extracellular Domain Nat.Struct.Mol.Biol. V. 21 976 2014.
ISSN: ISSN 1545-9993
PubMed: 25282151
DOI: 10.1038/NSMB.2900