Calcium in PDB 4xjq: The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed

All present enzymatic activity of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed:
3.2.1.18;

The structure of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed, PDB code: 4xjq was solved by L.Dirr, I.El-Deeb, P.Guillon, C.Carroux, L.Chavas, M.Von Itzstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.78 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.430, 94.015, 105.395, 90.00, 90.00, 90.00
R / Rfree (%)	16.2 / 20.9

The binding sites of Calcium atom in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed (pdb code 4xjq). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed, PDB code: 4xjq:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:18.9 occ:1.00 O A:ASP279 2.2 19.1 1.0 O A:ALA316 2.3 16.5 1.0 O A:GLY284 2.3 21.4 1.0 O A:HOH830 2.4 23.5 1.0 O A:SER282 2.4 21.9 1.0 OD1 A:ASP279 2.4 17.1 1.0 OG A:SER282 2.5 22.9 1.0 C A:ASP279 3.2 19.3 1.0 C A:SER282 3.3 23.1 1.0 C A:ALA316 3.5 16.8 1.0 C A:GLY284 3.5 20.0 1.0 CG A:ASP279 3.6 18.6 1.0 CB A:SER282 3.6 24.1 1.0 CA A:ASP279 3.7 19.7 1.0 CA A:SER282 3.9 23.7 1.0 O A:HOH894 3.9 26.9 1.0 O A:SER283 4.1 20.0 1.0 N A:SER282 4.1 23.5 1.0 CA A:ALA316 4.2 16.2 1.0 CA A:ILE285 4.2 18.4 1.0 C A:SER283 4.2 21.6 1.0 CB A:ASP279 4.3 19.3 1.0 N A:ILE285 4.3 19.9 1.0 N A:TYR280 4.4 19.4 1.0 N A:SER283 4.4 21.9 1.0 N A:GLY284 4.5 20.1 1.0 N A:ALA317 4.5 15.5 1.0 O A:HOH852 4.5 31.9 1.0 CA A:GLY284 4.6 21.6 1.0 OD2 A:ASP279 4.6 17.7 1.0 C A:ILE285 4.6 19.5 1.0 CA A:ALA317 4.7 14.7 1.0 CB A:ALA316 4.8 16.9 1.0 CA A:SER283 4.8 22.7 1.0 OE2 A:GLU286 4.8 23.1 1.0 N A:GLU286 4.8 19.7 1.0 CA A:TYR280 4.9 19.6 1.0 O A:SER278 4.9 21.4 1.0

Calcium binding site 2 out of 2 in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca601 b:23.6 occ:1.00 O B:ALA316 2.3 21.2 1.0 O B:GLY284 2.3 24.0 1.0 O B:ASP279 2.3 21.8 1.0 O B:HOH943 2.3 25.4 1.0 O B:SER282 2.4 27.0 1.0 OD1 B:ASP279 2.4 18.6 1.0 OG B:SER282 2.5 26.4 1.0 C B:ASP279 3.3 21.1 1.0 C B:SER282 3.4 28.0 1.0 C B:ALA316 3.5 20.8 1.0 C B:GLY284 3.5 22.9 1.0 CG B:ASP279 3.6 20.4 1.0 CB B:SER282 3.7 26.1 1.0 CA B:ASP279 3.7 22.1 1.0 CA B:SER282 3.9 26.5 1.0 O B:HOH711 4.1 33.1 1.0 N B:SER282 4.1 26.3 1.0 O B:SER283 4.1 26.0 1.0 CA B:ALA316 4.2 21.2 1.0 CA B:ILE285 4.2 21.4 1.0 C B:SER283 4.3 26.3 1.0 CB B:ASP279 4.3 21.4 1.0 N B:ILE285 4.3 21.6 1.0 O B:HOH947 4.4 41.5 1.0 N B:SER283 4.4 27.6 1.0 N B:TYR280 4.5 21.3 1.0 N B:ALA317 4.5 19.4 1.0 N B:GLY284 4.5 24.6 1.0 OD2 B:ASP279 4.6 18.1 1.0 CA B:GLY284 4.6 24.0 1.0 C B:ILE285 4.6 22.7 1.0 CB B:ALA316 4.7 22.4 1.0 CA B:ALA317 4.7 19.0 1.0 CA B:SER283 4.8 28.9 1.0 OE2 B:GLU286 4.8 24.6 1.0 O B:SER278 4.8 25.2 1.0 N B:GLU286 4.8 22.1 1.0 CA B:TYR280 4.9 21.7 1.0 CB B:ALA317 5.0 19.4 1.0

L.Dirr, I.M.El-Deeb, P.Guillon, C.J.Carroux, L.M.G.Chavas, M.Von Itzstein. The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed. Angew.Chem.Int.Ed.Engl. 2015.
ISSN: ESSN 1521-3773