Sodium in PDB 6y9j: Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose

The structure of Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose, PDB code: 6y9j was solved by D.Hoffmann, R.Diderrich, M.Kock, S.Friederichs, V.Reithofer, L.-O.Essen, H.-U.Moesch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.55 / 1.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	74.220, 104.140, 69.090, 90.00, 90.00, 90.00
R / Rfree (%)	14.6 / 16.7

The structure of Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose also contains other interesting chemical elements:

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

The binding sites of Sodium atom in the Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose (pdb code 6y9j). 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 Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose, PDB code: 6y9j:

Sodium binding site 1 out of 1 in the Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Subtype-Switched Epithelial Adhesin 1 to 9 A Domain (EPA1-CBL2EPA9) From Candida Glabrata in Complex with Beta- Lactose within 5.0Å range: probe atom residue distance (Å) B Occ A:Na305 b:31.7 occ:0.43 O A:LYS101 2.2 12.7 1.0 O A:HOH633 3.1 15.8 1.0 C A:LYS101 3.4 10.8 1.0 HA A:VAL102 3.5 14.5 0.8 HG12 A:VAL102 3.6 20.6 0.8 H A:LYS101 3.6 12.7 0.3 H A:LYS101 3.6 12.7 0.7 HA A:VAL102 3.7 15.2 0.2 HB3 A:LYS101 3.9 13.6 0.3 HB3 A:LYS101 4.0 14.2 0.7 O A:HOH707 4.1 32.9 1.0 N A:VAL102 4.3 10.3 0.8 N A:VAL102 4.3 11.6 0.2 CA A:VAL102 4.3 12.1 0.8 CA A:LYS101 4.3 10.1 0.7 N A:LYS101 4.3 10.6 1.0 CA A:LYS101 4.3 10.7 0.3 CA A:VAL102 4.4 12.7 0.2 CG1 A:VAL102 4.4 17.2 0.8 O A:HOH694 4.4 42.2 1.0 HG13 A:VAL102 4.5 20.6 0.8 O A:HOH606 4.6 22.2 1.0 CB A:LYS101 4.6 11.3 0.3 CB A:LYS101 4.6 11.8 0.7 HG2 A:LYS101 4.7 14.7 0.7 HB A:VAL102 4.9 18.2 0.2 HG2 A:LYS101 5.0 13.6 0.3 CB A:VAL102 5.0 15.8 0.8

D.Hoffmann, R.Diderrich, V.Reithofer, S.Friederichs, M.Kock, L.O.Essen, H.U.Mosch. Functional Reprogramming Ofcandida Glabrataepithelial Adhesins: the Role of Conserved and Variable Structural Motifs in Ligand Binding. J.Biol.Chem. V. 295 12512 2020.
ISSN: ESSN 1083-351X
PubMed: 32669365
DOI: 10.1074/JBC.RA120.013968