Sodium in PDB 2xju: X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose

The structure of X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose, PDB code: 2xju was solved by M.Veelders, S.Brueckner, D.Ott, C.Unverzagt, H.-U.Moesch, L.-O.Essen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.40 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.470, 62.570, 105.770, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.7

The structure of X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Calcium	(Ca)	2 atoms

The binding sites of Sodium atom in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose (pdb code 2xju). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose, PDB code: 2xju:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1273 b:18.9 occ:1.00 O A:HOH2218 2.1 7.0 0.5 OD1 A:ASP82 2.2 16.1 1.0 O A:HOH2186 2.4 30.8 1.0 OD1 A:ASN84 2.5 8.3 1.0 O A:HOH2380 2.5 14.2 1.0 O A:HOH2187 2.6 23.8 1.0 O A:HOH2223 2.8 27.6 1.0 CG A:ASP82 3.3 15.9 1.0 CG A:ASN84 3.4 8.1 1.0 O A:HOH2089 3.5 2.0 0.2 ND2 A:ASN84 3.6 10.8 1.0 O A:HOH2217 3.7 9.3 0.5 OD2 A:ASP82 3.8 19.4 1.0 N A:GLN98 4.5 7.3 1.0 OG1 A:THR230 4.5 11.7 1.0 O A:TYR83 4.6 8.0 1.0 CB A:ASP82 4.6 11.6 1.0 C A:ASP82 4.6 10.5 1.0 O A:HOH2189 4.7 24.6 1.0 O A:HOH2221 4.7 23.8 1.0 CD1 A:TRP228 4.7 6.6 1.0 CA A:ASP82 4.7 11.1 1.0 CA A:PRO97 4.7 7.9 1.0 CB A:ASN84 4.8 7.4 1.0 O A:ASP82 4.8 12.3 1.0 C A:TYR83 4.9 8.3 1.0 N A:TYR83 4.9 9.2 1.0 OE1 A:GLU99 5.0 13.0 1.0 O A:HOH2190 5.0 44.4 1.0

Sodium binding site 2 out of 2 in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae with Mutation S227A in Complex with Calcium and A1,2-Mannobiose within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1275 b:16.4 occ:1.00 O A:HOH2194 3.0 14.1 1.0 O A:HOH2120 3.0 29.6 1.0 O A:HOH2213 3.1 42.6 1.0 N A:PRO95 3.5 8.8 1.0 CB A:PRO86 3.6 7.0 1.0 C A:PHE94 3.8 9.0 1.0 CD A:PRO95 3.8 9.1 1.0 CA A:PRO86 3.8 7.0 1.0 CG A:PRO86 3.9 8.6 1.0 CA A:PRO95 3.9 8.0 1.0 O A:HOH2267 4.1 41.2 1.0 CG2 A:THR93 4.1 13.2 1.0 CA A:PHE94 4.1 9.6 1.0 CB A:PRO95 4.3 7.7 1.0 O A:PHE94 4.3 8.5 1.0 N A:PRO86 4.3 6.6 1.0 O A:THR93 4.4 12.0 1.0 N A:PHE94 4.4 10.4 1.0 O A:HOH2260 4.4 34.8 1.0 C A:THR93 4.5 12.3 1.0 CG A:PRO95 4.6 9.2 1.0 CD A:PRO86 4.7 6.8 1.0 O A:HOH2192 4.8 10.2 1.0 O A:HOH2057 4.9 41.3 1.0

M.Veelders, S.Brueckner, D.Ott, C.Unverzagt, H.-U.Moesch, L.-O.Essen. Structural Basis of Flocculin-Mediated Social Behavior in Yeast Proc.Natl.Acad.Sci.Usa V. 107 22511 2010.
ISSN: ISSN 0027-8424
PubMed: 21149680
DOI: 10.1073/PNAS.1013210108