Sodium in PDB 4aqp: The Structure of the Axh Domain of Ataxin-1.

The structure of The Structure of the Axh Domain of Ataxin-1., PDB code: 4aqp was solved by M.Rees, Y.W.Chen, C.De Chiara, A.Pastore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.916 / 2.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.539, 82.699, 137.110, 90.00, 90.00, 90.00
R / Rfree (%)	21.75 / 26.72

The binding sites of Sodium atom in the The Structure of the Axh Domain of Ataxin-1. (pdb code 4aqp). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the The Structure of the Axh Domain of Ataxin-1., PDB code: 4aqp:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in the The Structure of the Axh Domain of Ataxin-1.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Structure of the Axh Domain of Ataxin-1. within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1690 b:96.4 occ:1.00 O B:ALA603 2.2 88.8 1.0 O B:SER606 2.3 95.2 1.0 O B:LEU609 2.4 75.7 1.0 C B:ALA603 3.4 85.9 1.0 C B:SER606 3.4 96.3 1.0 C B:LEU609 3.5 72.6 1.0 CA B:ASN607 3.8 98.5 1.0 N B:ASN607 4.0 98.6 1.0 C B:ASN607 4.1 94.4 1.0 CA B:GLU604 4.1 90.2 1.0 N B:LEU609 4.1 80.8 1.0 CA B:LEU609 4.2 74.6 1.0 N B:GLU604 4.2 87.0 1.0 O B:ASN607 4.2 92.3 1.0 CB B:LEU609 4.4 71.7 1.0 CA B:ALA603 4.4 80.4 1.0 C B:GLU604 4.4 92.7 1.0 N B:LYS610 4.5 67.7 1.0 N B:SER606 4.5 96.1 1.0 CA B:SER606 4.5 96.7 1.0 OD1 B:ASN607 4.6 0.6 1.0 CA B:LYS610 4.7 66.4 1.0 O B:GLU604 4.7 94.8 1.0 CB B:ALA603 4.8 77.0 1.0 N B:ASP608 4.8 93.1 1.0 N B:ILE605 4.9 93.3 1.0

Sodium binding site 2 out of 3 in the The Structure of the Axh Domain of Ataxin-1.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of The Structure of the Axh Domain of Ataxin-1. within 5.0Å range: probe atom residue distance (Å) B Occ C:Na1690 b:59.3 occ:1.00 NZ C:LYS689 2.1 65.3 1.0 O C:ALA603 2.1 43.4 1.0 O C:SER606 2.4 58.2 1.0 O B:HOH2013 2.4 32.8 1.0 O C:LEU609 2.4 48.3 1.0 CE C:LYS689 2.6 63.8 1.0 C C:ALA603 3.3 42.2 1.0 C C:SER606 3.6 56.7 1.0 C C:LEU609 3.6 43.5 1.0 O B:HOH2015 4.0 50.3 1.0 CA C:ALA603 4.1 38.3 1.0 O C:GLU604 4.1 50.2 1.0 CD C:LYS689 4.1 63.1 1.0 O B:GLY655 4.3 36.5 1.0 N C:GLU604 4.3 41.6 1.0 C C:GLU604 4.4 47.2 1.0 CA C:LYS610 4.4 35.9 1.0 CA C:GLU604 4.4 43.9 1.0 N C:SER606 4.5 52.6 1.0 N C:LYS610 4.5 38.5 1.0 CA C:SER606 4.5 53.4 1.0 N C:LEU609 4.5 46.3 1.0 N C:ASN607 4.6 59.6 1.0 CB C:ALA603 4.6 37.6 1.0 CA C:ASN607 4.6 62.6 1.0 CA C:LEU609 4.6 43.6 1.0 CB C:SER606 4.8 53.6 1.0 OE1 B:GLN656 4.8 39.7 1.0 C C:ASN607 4.8 59.2 1.0 CB C:LYS610 4.9 36.5 1.0 CG B:GLN656 4.9 34.7 1.0 O C:ASN607 5.0 58.6 1.0

Sodium binding site 3 out of 3 in the The Structure of the Axh Domain of Ataxin-1.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of The Structure of the Axh Domain of Ataxin-1. within 5.0Å range: probe atom residue distance (Å) B Occ D:Na1690 b:67.3 occ:1.00 O D:SER606 2.4 88.1 1.0 O D:LEU609 2.5 69.3 1.0 O D:ALA603 2.6 76.7 1.0 C D:SER606 3.6 88.9 1.0 C D:LEU609 3.7 66.5 1.0 C D:ALA603 3.8 74.3 1.0 O D:ASN607 4.1 93.8 1.0 C D:ASN607 4.2 92.3 1.0 CA D:ASN607 4.2 94.2 1.0 N D:LEU609 4.3 74.4 1.0 N D:ASN607 4.4 91.4 1.0 CA D:LEU609 4.5 68.0 1.0 CA D:ALA603 4.6 71.0 1.0 N D:LYS610 4.6 62.8 1.0 CA D:SER606 4.7 86.6 1.0 CA D:LYS610 4.7 62.5 1.0 N D:GLU604 4.7 74.2 1.0 N D:SER606 4.8 84.1 1.0 O D:GLU604 4.8 83.7 1.0 N D:ASP608 4.8 88.9 1.0 CA D:GLU604 4.8 76.8 1.0 C D:GLU604 4.9 79.8 1.0 CB D:SER606 5.0 84.2 1.0

C.De Chiara, M.Rees, R.P.Menon, K.Pauwels, C.Lawrence, P.V.Konarev, D.I.Svergun, S.R.Martin, Y.W.Chen, A.Pastore. Self-Assembly and Conformational Heterogeneity of the Axh Domain of Ataxin-1: An Unusual Example of A Chameleon Fold Biophys.J. V. 104 1304 2013.
ISSN: ISSN 0006-3495
PubMed: 23528090
DOI: 10.1016/J.BPJ.2013.01.048