Calcium in PDB 4cpl: Structure of the Neuraminidase From the B/Brisbane/60/2008 Virus.

All present enzymatic activity of Structure of the Neuraminidase From the B/Brisbane/60/2008 Virus.:
3.2.1.18;

The structure of Structure of the Neuraminidase From the B/Brisbane/60/2008 Virus., PDB code: 4cpl was solved by S.G.Vachieri, P.J.Collins, V.Escuret, J.S.Casalegno, N.Cattle, O.Ferraris, M.Sabatier, E.Frobert, V.Caro, J.J.Skehel, S.J.Gamblin, F.Valla, M.Valette, M.Ottmann, J.W.Mccauley, R.S.Daniels, B.Lina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.126 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	159.784, 159.784, 91.592, 90.00, 90.00, 120.00
R / Rfree (%)	13.75 / 16.09

The binding sites of Calcium atom in the Structure of the Neuraminidase From the B/Brisbane/60/2008 Virus. (pdb code 4cpl). 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 Neuraminidase From the B/Brisbane/60/2008 Virus., PDB code: 4cpl:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of the Neuraminidase From the B/Brisbane/60/2008 Virus.


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 Neuraminidase From the B/Brisbane/60/2008 Virus. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca500 b:19.4 occ:1.00 OD2 A:ASP323 2.3 22.1 1.0 O A:ASP292 2.3 19.4 1.0 O A:GLY345 2.3 16.6 1.0 O A:HOH2294 2.3 20.0 1.0 O A:GLY343 2.4 17.6 1.0 O A:THR296 2.5 17.1 1.0 C A:GLY343 3.4 18.2 1.0 CG A:ASP323 3.5 23.2 1.0 C A:THR296 3.5 17.5 1.0 C A:GLY345 3.5 17.3 1.0 C A:ASP292 3.5 18.2 1.0 O A:HOH2289 4.0 19.6 1.0 CA A:GLY346 4.0 15.8 1.0 CA A:GLY343 4.0 18.9 1.0 CA A:ALA297 4.2 17.5 1.0 CA A:ASN293 4.2 16.1 1.0 N A:ALA297 4.2 17.8 1.0 N A:GLY346 4.2 16.2 1.0 N A:ASN293 4.3 15.8 1.0 CB A:ASP323 4.3 16.8 1.0 OD1 A:ASP323 4.3 19.5 1.0 N A:THR296 4.4 17.8 1.0 C A:ASN293 4.4 18.2 1.0 C A:SER344 4.4 24.8 1.0 N A:GLY345 4.4 19.5 1.0 N A:SER344 4.5 20.4 1.0 CA A:THR296 4.6 17.9 1.0 CA A:ASP292 4.6 17.3 1.0 CA A:GLY345 4.6 19.5 1.0 N A:SER294 4.6 18.4 0.5 N A:SER294 4.6 18.4 0.5 O A:SER344 4.7 18.1 1.0 O A:LYS342 4.7 22.7 1.0 CB A:ASP292 4.7 18.7 1.0 N A:ASP292 4.8 15.3 1.0 CA A:SER344 4.8 23.2 1.0 O A:ASN293 4.8 20.0 1.0 O A:PRO325 4.8 19.2 1.0 OD1 A:ASP292 5.0 19.6 1.0

Calcium binding site 2 out of 2 in the Structure of the Neuraminidase From the B/Brisbane/60/2008 Virus.


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 Neuraminidase From the B/Brisbane/60/2008 Virus. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca500 b:23.1 occ:1.00 O B:ASP292 2.3 18.1 1.0 O B:HOH2228 2.4 21.6 1.0 OD2 B:ASP323 2.4 20.2 1.0 O B:GLY345 2.4 19.1 1.0 O B:GLY343 2.4 20.1 1.0 O B:THR296 2.5 17.5 1.0 C B:GLY343 3.5 19.9 1.0 C B:ASP292 3.5 21.0 1.0 C B:THR296 3.5 19.8 1.0 C B:GLY345 3.5 21.1 1.0 CG B:ASP323 3.6 22.8 1.0 O B:HOH2223 3.9 20.4 1.0 CA B:GLY346 4.1 16.3 1.0 CA B:GLY343 4.1 18.6 1.0 CA B:ASN293 4.2 20.4 1.0 CA B:ALA297 4.2 17.5 1.0 N B:ALA297 4.2 18.7 1.0 N B:GLY346 4.2 17.2 1.0 N B:ASN293 4.3 18.3 1.0 N B:GLY345 4.3 25.1 1.0 CB B:ASP323 4.3 18.4 1.0 C B:ASN293 4.4 22.6 1.0 N B:THR296 4.4 18.9 1.0 C B:SER344 4.4 24.4 1.0 OD1 B:ASP323 4.4 20.2 1.0 N B:SER344 4.5 21.5 1.0 CA B:ASP292 4.6 18.2 1.0 CA B:THR296 4.6 19.7 1.0 CA B:GLY345 4.6 21.8 1.0 N B:SER294 4.7 19.8 1.0 CB B:ASP292 4.7 16.8 1.0 O B:LYS342 4.8 24.1 1.0 N B:ASP292 4.8 16.9 1.0 CA B:SER344 4.8 25.0 1.0 O B:ASN293 4.8 20.2 1.0 O B:SER344 4.8 25.9 1.0 O B:PRO325 4.9 18.8 1.0 OD1 B:ASP292 5.0 24.4 1.0

V.Escuret, P.J.Collins, J.Casalegno, S.G.Vachieri, N.Cattle, O.Ferraris, M.Sabatier, E.Frobert, V.Caro, J.J.Skehel, S.Gamblin, F.Valla, M.Valette, M.Ottmann, J.W.Mccauley, R.S.Daniels, B.Lina. A Novel I221 L Substitution in Neuraminidase Confers High Level Resistance to Oseltamivir in Influenza B Viruses. J.Infect.Dis. V. 210 1260 2014.
ISSN: ISSN 1537-6613
PubMed: 24795482
DOI: 10.1093/INFDIS/JIU244