Calcium in PDB 4a3x: Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose

The structure of Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose, PDB code: 4a3x was solved by F.S.Ielasi, K.Decanniere, R.G.Willaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.02 / 1.65
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	75.481, 105.453, 69.571, 90.00, 90.00, 90.00
R / Rfree (%)	17.17 / 20.969

The binding sites of Calcium atom in the Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose (pdb code 4a3x). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose, PDB code: 4a3x:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose


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 EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1267 b:14.8 occ:1.00 O A:HOH2011 2.3 14.8 1.0 O A:HOH2016 2.4 17.4 1.0 OG1 A:THR55 2.5 12.9 1.0 O A:HOH2012 2.5 15.9 1.0 OD2 A:ASP53 2.5 15.8 1.0 OD1 A:ASP53 2.6 15.2 1.0 CG A:ASP53 2.9 19.1 1.0 CB A:THR55 3.5 13.9 1.0 O A:HOH2139 4.3 16.4 1.0 N A:THR55 4.4 15.6 1.0 CB A:ASP53 4.4 14.8 1.0 CG2 A:THR55 4.4 14.8 1.0 CA A:THR55 4.5 13.4 1.0 O A:HOH2020 4.7 17.1 1.0 CG2 A:THR258 4.7 16.3 1.0 O A:HOH2137 4.7 14.8 1.0 O A:HOH2014 4.7 17.0 1.0 O A:HOH2013 4.7 25.9 1.0 O A:HOH2009 4.8 14.1 1.0 O A:HOH2010 4.8 13.8 1.0

Calcium binding site 2 out of 2 in the Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the N-Terminal Domain of the EPA1 Adhesin (EPA1-Np) From the Pathogenic Yeast Candida Glabrata, in Complex with Calcium and Lactose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1268 b:10.5 occ:1.00 O A:ASP229 2.3 9.4 1.0 OD1 A:ASN225 2.4 9.7 1.0 O A:GLU227 2.4 12.3 1.0 OD1 A:ASP164 2.4 10.7 1.0 O3 A:LAT1269 2.4 11.0 1.0 OD2 A:ASP165 2.5 10.2 1.0 O4 A:LAT1269 2.6 10.4 1.0 CG A:ASP164 3.3 9.7 1.0 C4 A:LAT1269 3.3 12.8 1.0 C3 A:LAT1269 3.4 13.3 1.0 CG A:ASP165 3.4 9.1 1.0 CG A:ASN225 3.5 10.8 1.0 C A:GLU227 3.6 10.9 1.0 C A:ASP229 3.6 8.7 1.0 OD2 A:ASP164 3.7 11.8 1.0 OD1 A:ASP165 3.7 10.5 1.0 N A:GLU227 4.0 10.2 1.0 ND2 A:ASN225 4.0 10.6 1.0 C2 A:LAT1269 4.0 14.4 1.0 N A:ASP229 4.2 9.9 1.0 C A:TYR228 4.2 12.1 1.0 N A:ARG226 4.3 10.2 1.0 O A:TYR228 4.4 11.5 1.0 C A:ASP164 4.4 10.2 1.0 CA A:GLU227 4.4 11.4 1.0 N A:ASP165 4.4 9.2 1.0 CA A:ASP229 4.5 10.7 1.0 O A:ASP164 4.5 10.4 1.0 N A:TYR228 4.6 10.6 1.0 CB A:ASP164 4.6 10.7 1.0 N A:GLY230 4.6 10.7 1.0 CB A:ASP165 4.6 7.3 1.0 CA A:GLY230 4.7 10.9 1.0 CA A:TYR228 4.7 10.9 1.0 CB A:ASN225 4.7 9.5 1.0 CG A:ARG226 4.7 10.6 1.0 CB A:TYR228 4.7 12.8 1.0 C5 A:LAT1269 4.8 16.3 1.0 CA A:ASN225 4.8 8.4 1.0 CA A:ASP165 4.9 8.2 1.0 O2 A:LAT1269 4.9 14.2 1.0 CA A:ASP164 4.9 9.8 1.0 C A:ASN225 5.0 9.1 1.0

F.S.Ielasi, K.Decanniere, R.G.Willaert. The Epithelial Adhesin 1 (EPA1P) From the Human-Pathogenic Yeast Candida Glabrata : Structural and Functional Study of the Carbohydrate-Binding Domain Acta Crystallogr.,Sect.D V. 68 210 2012.
ISSN: ISSN 0907-4449
PubMed: 22349222
DOI: 10.1107/S0907444911054898