Calcium in PDB 2htv: N4 Neuraminidase

The structure of N4 Neuraminidase, PDB code: 2htv was solved by R.J.Russell, L.F.Haire, D.J.Stevens, P.J.Collins, Y.P.Lin, G.M.Blackburn, A.J.Hay, S.J.Gamblin, J.J.Skehel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.80
Space group	P 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	193.790, 193.790, 193.790, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 27.3

The binding sites of Calcium atom in the N4 Neuraminidase (pdb code 2htv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the N4 Neuraminidase, PDB code: 2htv:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the N4 Neuraminidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of N4 Neuraminidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca995 b:19.7 occ:1.00 O A:TYR347 2.2 32.0 1.0 O A:GLY297 2.5 18.3 1.0 O A:ASP293 2.6 18.2 1.0 OD1 A:ASP324 2.7 26.8 1.0 O A:GLY345 2.8 36.4 1.0 O A:ARG346 3.1 40.1 1.0 C A:TYR347 3.4 31.1 1.0 C A:GLY297 3.5 17.9 1.0 C A:GLY345 3.6 37.1 1.0 CG A:ASP324 3.8 26.8 1.0 C A:ASP293 3.8 18.8 1.0 C A:ARG346 3.8 37.2 1.0 CA A:GLY348 4.0 24.9 1.0 O A:HOH1172 4.1 19.3 1.0 N A:GLY297 4.2 20.1 1.0 CA A:GLY345 4.2 36.2 1.0 N A:GLY348 4.2 27.7 1.0 N A:SER298 4.3 16.9 1.0 CA A:SER298 4.4 15.2 1.0 CA A:GLY297 4.4 18.3 1.0 N A:TYR347 4.4 34.9 1.0 N A:ARG346 4.4 37.7 1.0 CA A:TYR347 4.4 32.9 1.0 CA A:ASN294 4.5 18.4 1.0 CB A:ASP324 4.5 25.4 1.0 O A:LYS344 4.6 35.5 1.0 N A:ASN294 4.6 18.0 1.0 OD2 A:ASP324 4.6 28.8 1.0 CA A:ARG346 4.7 37.5 1.0 O A:PRO326 4.7 22.5 1.0 CA A:ASP293 4.8 18.9 1.0 C A:ASN294 4.9 18.9 1.0 CB A:ASP293 4.9 19.3 1.0

Calcium binding site 2 out of 2 in the N4 Neuraminidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of N4 Neuraminidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca993 b:26.4 occ:1.00 O B:TYR347 2.3 36.3 1.0 O B:GLY297 2.3 22.6 1.0 O B:GLY345 2.3 37.0 1.0 O B:ASP293 2.4 22.8 1.0 OD1 B:ASP324 2.5 26.6 1.0 O B:ARG346 2.9 44.7 1.0 C B:GLY297 3.4 22.5 1.0 C B:TYR347 3.4 35.5 1.0 C B:GLY345 3.5 38.5 1.0 C B:ASP293 3.6 23.3 1.0 CG B:ASP324 3.7 26.3 1.0 O B:HOH1183 3.7 21.9 1.0 C B:ARG346 3.7 42.1 1.0 CA B:GLY348 4.1 30.9 1.0 N B:GLY297 4.1 23.5 1.0 CA B:ASN294 4.2 23.6 1.0 CA B:GLY297 4.3 22.5 1.0 N B:GLY348 4.3 33.4 1.0 N B:SER298 4.3 21.6 1.0 CA B:GLY345 4.3 38.8 1.0 N B:ASN294 4.3 23.0 1.0 N B:TYR347 4.4 39.6 1.0 OD2 B:ASP324 4.4 26.0 1.0 CA B:TYR347 4.4 37.7 1.0 CA B:SER298 4.4 20.4 1.0 N B:ARG346 4.5 39.9 1.0 CA B:ARG346 4.6 41.8 1.0 CA B:ASP293 4.6 23.5 1.0 CB B:ASP324 4.6 25.5 1.0 O B:LYS344 4.7 39.3 1.0 C B:ASN294 4.7 23.3 1.0 N B:ASP293 4.8 23.1 1.0 CB B:ASP293 4.8 25.2 1.0 O B:PRO326 4.8 24.4 1.0 OD2 B:ASP293 5.0 28.0 1.0

R.J.Russell, L.F.Haire, D.J.Stevens, P.J.Collins, Y.P.Lin, G.M.Blackburn, A.J.Hay, S.J.Gamblin, J.J.Skehel. The Structure of H5N1 Avian Influenza Neuraminidase Suggests New Opportunities For Drug Design. Nature V. 443 45 2006.
ISSN: ISSN 0028-0836
PubMed: 16915235
DOI: 10.1038/NATURE05114