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Sodium in PDB 4lhl: Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae

Protein crystallography data

The structure of Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae, PDB code: 4lhl was solved by F.S.Ielasi, R.G.Willaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.38 / 1.43
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.800, 61.770, 106.730, 90.00, 90.00, 90.00
R / Rfree (%) 13.2 / 16.5

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae (pdb code 4lhl). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae, PDB code: 4lhl:

Sodium binding site 1 out of 1 in 4lhl

Go back to Sodium Binding Sites List in 4lhl
Sodium binding site 1 out of 1 in the Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na301

b:8.5
occ:1.00
O A:TRP228 2.3 9.5 1.0
O A:VAL226 2.3 8.3 1.0
OD1 A:ASN224 2.3 10.8 1.0
O A:HOH428 2.4 15.1 1.0
OD1 A:ASP161 2.4 12.3 1.0
CG A:ASP161 3.1 10.6 1.0
OD2 A:ASP161 3.3 12.4 1.0
CG A:ASN224 3.3 9.1 1.0
C A:TRP228 3.5 7.5 1.0
C A:VAL226 3.5 7.6 1.0
ND2 A:ASN224 3.6 8.7 1.0
N A:TRP228 4.0 8.1 1.0
C A:SER227 4.1 8.0 1.0
N A:VAL226 4.1 8.3 1.0
O A:HOH554 4.1 34.4 1.0
CB A:ASP160 4.2 12.2 1.0
OG A:SER227 4.2 9.9 1.0
O A:HOH596 4.3 28.2 1.0
O A:SER227 4.3 8.6 1.0
CA A:TRP228 4.3 7.5 1.0
O A:HOH526 4.4 24.6 1.0
CA A:VAL226 4.4 8.2 1.0
C A:ASP160 4.4 10.1 1.0
CB A:ASP161 4.5 11.3 1.0
CG1 A:VAL226 4.5 13.2 1.0
N A:GLY229 4.5 8.8 1.0
N A:SER227 4.5 7.4 1.0
O A:ASP160 4.6 9.8 1.0
N A:ASP161 4.6 9.1 1.0
CA A:GLY229 4.7 10.2 1.0
CA A:SER227 4.7 7.6 1.0
CB A:ASN224 4.7 8.2 1.0
N A:ALA225 4.7 9.0 1.0
CA A:ASP160 4.8 11.1 1.0
CA A:ASP161 5.0 8.5 1.0
CB A:TRP228 5.0 8.6 1.0

Reference:

K.Goossens, F.S.Ielasi, R.G.Willaert. Molecular Mechanism of Flocculation Self-Recognition in Yeast and Its Role in Mating and Survival To Be Published.
Page generated: Mon Oct 7 16:47:57 2024

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