Calcium in PDB 4lhn: Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae, in Complex with Calcium and Mannose

The structure of Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae, in Complex with Calcium and Mannose, PDB code: 4lhn 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)	15.03 / 2.12
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.700, 63.590, 106.540, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 19.4

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

Calcium 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, in Complex with Calcium and Mannose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the N-Terminal Domain of the FLO1 Adhesin (N-FLO1P) From the Yeast Saccharomyces Cerevisiae, in Complex with Calcium and Mannose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca302 b:14.4 occ:1.00 OD1 A:ASP160 2.3 17.4 1.0 O A:TRP228 2.3 15.1 1.0 OD1 A:ASN224 2.4 14.3 1.0 OD2 A:ASP161 2.4 14.3 1.0 O A:VAL226 2.5 13.4 1.0 O4 A:MAN301 2.6 17.4 1.0 O3 A:MAN301 2.6 19.0 1.0 CG A:ASP160 3.2 16.6 1.0 CG A:ASP161 3.3 16.4 1.0 C4 A:MAN301 3.4 19.2 1.0 C3 A:MAN301 3.4 18.9 1.0 CG A:ASN224 3.5 14.5 1.0 C A:TRP228 3.5 14.0 1.0 C A:VAL226 3.6 13.9 1.0 OD2 A:ASP160 3.6 17.4 1.0 OD1 A:ASP161 3.6 20.7 1.0 N A:VAL226 4.0 15.3 1.0 N A:TRP228 4.0 12.9 1.0 ND2 A:ASN224 4.0 14.3 1.0 C A:SER227 4.1 12.8 1.0 CA A:TRP228 4.2 13.8 1.0 O A:SER227 4.3 12.7 1.0 C A:ASP160 4.4 15.2 1.0 CA A:VAL226 4.4 14.0 1.0 N A:ALA225 4.4 14.3 1.0 N A:ASP161 4.4 15.0 1.0 CG1 A:VAL226 4.5 15.4 1.0 O A:ASP160 4.5 15.2 1.0 CB A:ASP160 4.5 15.9 1.0 N A:GLY229 4.5 14.7 1.0 CB A:ASP161 4.5 16.2 1.0 N A:SER227 4.6 13.3 1.0 OG A:SER227 4.6 14.3 1.0 CB A:ASN224 4.7 14.0 1.0 CA A:GLY229 4.8 15.6 1.0 CA A:ASN224 4.8 14.3 1.0 CA A:SER227 4.8 13.4 1.0 C5 A:MAN301 4.8 20.4 1.0 C2 A:MAN301 4.8 19.4 1.0 CA A:ASP161 4.9 15.4 1.0 CB A:TRP228 4.9 14.2 1.0 CA A:ASP160 4.9 17.2 1.0

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.