Calcium in PDB 8slv: Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti.

All present enzymatic activity of Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti.:
3.2.1.20;

The structure of Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti., PDB code: 8slv was solved by A.G.Gittis, A.E.Williams, D.Garboczi, E.Calvo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.55 / 2.32
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	48.76, 51.03, 70.75, 101.82, 94.66, 95.76
R / Rfree (%)	14.6 / 18.8

The structure of Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti. also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Calcium atom in the Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti. (pdb code 8slv). 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 A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti., PDB code: 8slv:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca611 b:31.2 occ:1.00 OD1 A:ASP39 2.1 20.4 1.0 O A:ILE43 2.2 18.9 1.0 OD2 A:ASP45 2.2 17.4 1.0 OD1 A:ASP37 2.2 21.5 1.0 O A:HOH714 2.3 16.8 1.0 OD1 A:ASP41 2.4 20.6 1.0 CG A:ASP39 3.2 26.0 1.0 CG A:ASP41 3.2 21.3 1.0 CG A:ASP45 3.3 18.1 1.0 CG A:ASP37 3.3 20.7 1.0 C A:ILE43 3.4 19.9 1.0 OD2 A:ASP41 3.5 22.7 1.0 OD2 A:ASP39 3.5 27.4 1.0 CB A:ASP45 3.7 15.7 1.0 N A:ASP39 4.0 21.5 1.0 N A:SER38 4.1 19.8 1.0 N A:ILE43 4.1 19.6 1.0 OD2 A:ASP37 4.1 20.0 1.0 CA A:ILE43 4.1 17.9 1.0 CA A:ASP37 4.2 18.5 1.0 CB A:ASP37 4.2 18.2 1.0 CB A:ILE43 4.2 17.3 1.0 C A:GLY44 4.3 17.5 1.0 O A:GLU90 4.4 20.3 1.0 OD1 A:ASP45 4.4 20.2 1.0 N A:ASP45 4.4 18.2 1.0 N A:GLY44 4.4 18.6 1.0 CB A:ASP39 4.4 21.4 1.0 N A:ASP41 4.5 17.7 1.0 O A:GLY44 4.5 13.8 1.0 CA A:GLY44 4.6 14.5 1.0 CB A:ASP41 4.6 18.7 1.0 CA A:ASP39 4.6 25.6 1.0 C A:ASP37 4.6 19.6 1.0 CA A:ASP45 4.7 15.1 1.0 N A:GLY40 4.7 18.9 1.0 C A:ASP39 4.8 19.4 1.0 CG2 A:ILE43 4.9 18.5 1.0 CA A:ASP41 5.0 21.0 1.0

Calcium binding site 2 out of 2 in the Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of A Salivary Alpha-Glucosidase From the Mosquito Vector Aedes Aegypti. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca612 b:14.9 occ:1.00 OD2 A:ASP189 2.4 17.9 1.0 O A:LEU224 2.4 16.1 1.0 OE2 A:GLU226 2.4 12.0 1.0 O A:HOH773 2.5 12.3 1.0 O A:TYR223 2.5 16.8 1.0 O A:HOH722 2.5 11.3 1.0 OD1 A:ASN118 2.5 16.0 1.0 C A:LEU224 3.3 18.9 1.0 CD A:GLU226 3.4 20.0 1.0 CG A:ASP189 3.4 18.3 1.0 CG A:ASN118 3.5 14.9 1.0 C A:TYR223 3.6 16.0 1.0 OE1 A:GLU226 3.6 18.1 1.0 CA A:LEU224 3.7 16.8 1.0 ND2 A:ASN118 3.9 11.0 1.0 CB A:ASP189 3.9 15.8 1.0 N A:LEU224 4.1 18.1 1.0 O A:ASN118 4.3 14.4 1.0 N A:PHE225 4.3 14.9 1.0 O A:HOH845 4.4 12.3 1.0 OD1 A:ASP189 4.4 18.2 1.0 O A:LEU190 4.4 13.3 1.0 OE1 A:GLN182 4.6 22.6 1.0 CD2 A:LEU180 4.8 14.7 1.0 CG A:GLU226 4.8 16.6 1.0 CB A:ASN118 4.8 14.0 1.0 CA A:PHE225 4.8 14.3 1.0 CA A:TYR223 4.8 13.6 1.0 C A:PHE225 4.9 16.7 1.0 CB A:TYR223 4.9 15.6 1.0 CA A:ASP189 5.0 14.4 1.0

A.E.Williams, A.G.Gittis, K.Botello, P.Cruz, I.Martin-Martin, P.C.Valenzuela Leon, B.Sumner, B.Bonilla, E.Calvo. Structural and Functional Comparisons of Salivary Alpha-Glucosidases From the Mosquito Vectors Aedes Aegypti, Anopheles Gambiae, and Culex Quinquefasciatus. Insect Biochem.Mol.Biol. V. 167 04097 2024.
ISSN: ISSN 0965-1748
PubMed: 38428508
DOI: 10.1016/J.IBMB.2024.104097