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Sodium in PDB 2xjq: X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae

Protein crystallography data

The structure of X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae, PDB code: 2xjq 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) 20.00 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.270, 61.580, 106.010, 90.00, 90.00, 90.00
R / Rfree (%) 14.247 / 17.821

Other elements in 2xjq:

The structure of X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae (pdb code 2xjq). 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, PDB code: 2xjq:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 2xjq

Go back to Sodium Binding Sites List in 2xjq
Sodium binding site 1 out of 2 in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1272

b:19.1
occ:1.00
O A:HOH2261 2.0 49.5 1.0
OD1 A:ASP82 2.2 20.9 1.0
O A:HOH2019 2.2 15.3 1.0
OD1 A:ASN84 2.3 12.5 1.0
O A:HOH2123 2.6 30.9 1.0
O A:HOH2090 3.4 22.3 1.0
CG A:ASN84 3.4 11.3 1.0
CG A:ASP82 3.4 19.6 1.0
ND2 A:ASN84 3.8 12.4 1.0
OD2 A:ASP82 3.9 23.9 1.0
O A:TYR83 4.3 11.3 1.0
N A:GLN98 4.3 13.0 1.0
OG1 A:THR230 4.3 14.4 1.0
CD1 A:TRP228 4.4 11.2 1.0
CB A:GLN98 4.5 14.9 1.0
C A:TYR83 4.6 10.9 1.0
C A:ASP82 4.6 15.6 1.0
CB A:ASP82 4.6 16.5 1.0
O A:GLY229 4.7 11.8 1.0
CB A:ASN84 4.7 10.9 1.0
N A:TYR83 4.7 12.7 1.0
CA A:ASP82 4.7 15.6 1.0
CG2 A:THR230 4.8 14.2 1.0
NE2 A:GLN98 4.9 20.2 1.0
CA A:PRO97 4.9 11.9 1.0
O A:HOH2202 4.9 33.3 1.0
N A:ASN84 4.9 11.2 1.0
CA A:ASN84 4.9 11.3 1.0
OE1 A:GLU99 5.0 14.9 0.8
O A:ASP82 5.0 19.6 1.0

Sodium binding site 2 out of 2 in 2xjq

Go back to Sodium Binding Sites List in 2xjq
Sodium binding site 2 out of 2 in the X-Ray Structure of the N-Terminal Domain of the Flocculin FLO5 From Saccharomyces Cerevisiae


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1274

b:10.6
occ:1.00
O A:TRP228 2.3 11.8 1.0
OD1 A:ASN224 2.3 11.5 1.0
O A:VAL226 2.3 9.7 1.0
O A:HOH2051 2.4 14.2 1.0
OD1 A:ASP161 2.4 13.6 1.0
CG A:ASP161 3.1 12.4 1.0
OD2 A:ASP161 3.2 13.4 1.0
CG A:ASN224 3.3 9.4 1.0
C A:TRP228 3.5 11.0 1.0
C A:VAL226 3.6 9.6 1.0
ND2 A:ASN224 3.6 9.8 1.0
N A:TRP228 4.0 10.9 1.0
N A:VAL226 4.1 10.2 1.0
C A:SER227 4.1 10.6 1.0
CB A:ASP160 4.2 12.7 1.0
O A:HOH2223 4.3 46.7 1.0
CA A:TRP228 4.3 10.3 1.0
OG A:SER227 4.3 11.9 1.0
O A:HOH2201 4.3 31.4 1.0
O A:SER227 4.3 9.3 1.0
C A:ASP160 4.4 11.5 1.0
O A:HOH2115 4.4 30.0 1.0
O A:HOH2113 4.4 21.4 1.0
CA A:VAL226 4.4 10.1 1.0
CB A:ASP161 4.4 11.6 1.0
CG1 A:VAL226 4.5 12.7 1.0
N A:GLY229 4.5 10.5 1.0
N A:SER227 4.6 9.7 1.0
O A:ASP160 4.6 11.1 1.0
N A:ASP161 4.6 10.9 1.0
CB A:ASN224 4.7 9.3 1.0
CA A:ASP160 4.7 12.8 1.0
CA A:GLY229 4.7 10.0 1.0
CA A:SER227 4.7 10.0 1.0
N A:ALA225 4.7 10.7 1.0
CA A:ASP161 4.9 11.2 1.0
CB A:TRP228 4.9 11.0 1.0

Reference:

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
Page generated: Tue Dec 15 05:59:23 2020

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