Calcium in PDB 4xjr: 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: 4xjr 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)	50.00 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.850, 98.303, 103.261, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 29.8

The structure of The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Calcium atom in the The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed (pdb code 4xjr). 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: 4xjr:
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:35.4 occ:1.00 O A:SER282 2.3 42.2 1.0 O A:GLY284 2.3 42.1 1.0 O A:ALA316 2.4 36.5 1.0 O A:ASP279 2.4 35.1 1.0 OD1 A:ASP279 2.5 48.3 1.0 OG A:SER282 2.5 42.9 1.0 C A:ASP279 3.3 39.0 1.0 C A:SER282 3.4 40.4 1.0 C A:ALA316 3.6 37.2 1.0 C A:GLY284 3.6 41.4 1.0 CG A:ASP279 3.6 44.2 1.0 CB A:SER282 3.7 42.0 1.0 CA A:ASP279 3.7 40.8 1.0 CA A:SER282 3.9 40.6 1.0 O A:SER283 4.2 41.9 1.0 C A:SER283 4.2 39.3 1.0 CA A:ILE285 4.2 40.4 1.0 N A:SER282 4.2 38.6 1.0 CB A:ASP279 4.3 41.8 1.0 N A:ILE285 4.4 40.7 1.0 CA A:ALA316 4.4 39.9 1.0 N A:SER283 4.4 39.1 1.0 N A:GLU286 4.4 45.0 1.0 N A:GLY284 4.5 40.4 1.0 C A:ILE285 4.5 41.7 1.0 N A:ALA317 4.5 37.1 1.0 N A:TYR280 4.5 38.6 1.0 OD2 A:ASP279 4.6 45.9 1.0 CA A:GLY284 4.6 40.0 1.0 CA A:ALA317 4.6 37.3 1.0 CA A:SER283 4.7 39.8 1.0 CB A:ALA317 4.7 37.5 1.0 O A:SER278 4.9 46.6 1.0 CB A:ALA316 4.9 40.0 1.0 N A:ASP279 5.0 42.3 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:55.4 occ:1.00 OD1 B:ASP279 2.2 55.1 1.0 O B:SER282 2.3 44.5 1.0 O B:ASP279 2.4 47.2 1.0 O B:ALA316 2.4 37.5 1.0 O B:GLY284 2.4 49.7 1.0 OG B:SER282 2.8 57.7 1.0 C B:SER282 3.3 48.3 1.0 CG B:ASP279 3.4 51.5 1.0 C B:ASP279 3.4 50.7 1.0 C B:GLY284 3.5 48.0 1.0 C B:ALA316 3.6 39.1 1.0 CA B:ASP279 3.8 52.0 1.0 CB B:SER282 3.9 54.1 1.0 O B:SER283 4.1 50.4 1.0 CA B:SER282 4.1 51.8 1.0 C B:SER283 4.1 50.5 1.0 CA B:ILE285 4.1 48.6 1.0 CB B:ASP279 4.2 51.2 1.0 OD2 B:ASP279 4.3 50.0 1.0 N B:ILE285 4.3 48.3 1.0 OE2 B:GLU286 4.3 60.3 1.0 N B:SER283 4.3 49.3 1.0 C B:ILE285 4.4 50.0 1.0 CA B:ALA316 4.4 39.1 1.0 N B:GLY284 4.5 49.2 1.0 CA B:SER283 4.5 54.4 1.0 N B:SER282 4.5 51.4 1.0 N B:GLU286 4.5 56.0 1.0 N B:TYR280 4.6 50.2 1.0 CA B:GLY284 4.6 48.6 1.0 N B:ALA317 4.6 38.4 1.0 CA B:ALA317 4.8 38.6 1.0 CB B:ALA316 4.9 39.1 1.0 O B:ILE285 4.9 44.5 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