Potassium in PDB 4c7w: Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid

All present enzymatic activity of Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid:
3.1.1.53;

The structure of Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid, PDB code: 4c7w was solved by Q.H.Zeng, E.G.Huizinga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.92 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.566, 106.590, 135.607, 90.00, 90.00, 90.00
R / Rfree (%)	21.371 / 24.877

The binding sites of Potassium atom in the Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid (pdb code 4c7w). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid, PDB code: 4c7w:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:K802 b:51.9 occ:1.00 OD1 A:ASP230 2.6 45.3 1.0 OG A:SER278 2.6 45.7 1.0 O A:LEU282 2.6 42.5 1.0 O A:SER231 2.8 45.4 1.0 O A:GLU280 3.1 46.5 1.0 OE1 A:GLN232 3.1 47.0 1.0 O A:HOH2030 3.3 48.7 1.0 C A:LEU282 3.5 43.6 1.0 C A:SER231 3.7 44.2 1.0 CB A:SER278 3.7 45.6 1.0 CG A:ASP230 3.8 44.8 1.0 O A:HOH2033 3.9 46.7 1.0 N A:SER231 4.0 45.3 1.0 CD A:GLN232 4.1 45.9 1.0 CB A:GLN232 4.1 41.6 1.0 N A:LEU283 4.2 43.9 1.0 N A:LEU282 4.2 45.9 1.0 C A:TYR281 4.2 46.8 1.0 C A:GLU280 4.2 48.0 1.0 OD2 A:ASP230 4.2 44.3 1.0 CA A:LEU283 4.3 42.2 1.0 O A:TYR281 4.3 47.6 1.0 N A:GLN232 4.4 43.0 1.0 CA A:GLN232 4.4 42.8 1.0 CA A:SER278 4.4 45.4 1.0 CA A:LEU282 4.5 45.6 1.0 CA A:SER231 4.5 44.8 1.0 N A:SER284 4.5 39.0 1.0 CG A:GLN232 4.6 42.4 1.0 CB A:TYR281 4.7 47.0 1.0 C A:LEU283 4.7 41.0 1.0 CA A:TYR281 4.8 48.1 1.0 OG A:SER284 4.9 36.5 1.0 C A:ASP230 4.9 45.0 1.0 N A:TYR281 5.0 48.7 1.0 CB A:ASP230 5.0 44.7 1.0 N A:GLU280 5.0 48.8 1.0 CA A:ASP230 5.0 46.0 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Mouse Hepatitis Virus Strain S Hemagglutinin-Esterase in Complex with 4-O-Acetylated Sialic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:K802 b:66.2 occ:1.00 OG B:SER278 2.5 55.7 1.0 OD1 B:ASP230 2.6 56.1 1.0 O B:LEU282 2.8 55.3 1.0 O B:SER231 2.9 54.5 1.0 O B:GLU280 3.1 57.4 1.0 OE1 B:GLN232 3.1 54.7 1.0 O B:HOH2016 3.3 55.6 1.0 C B:SER231 3.6 52.9 1.0 CG B:ASP230 3.6 57.4 1.0 CB B:SER278 3.7 54.9 1.0 C B:LEU282 3.8 56.9 1.0 N B:SER231 4.0 55.7 1.0 OD2 B:ASP230 4.1 57.7 1.0 CB B:GLN232 4.1 49.4 1.0 CD B:GLN232 4.2 52.6 1.0 N B:GLN232 4.2 50.7 1.0 C B:GLU280 4.3 59.2 1.0 CA B:GLN232 4.3 49.8 1.0 C B:TYR281 4.3 59.8 1.0 O B:TYR281 4.3 59.5 1.0 N B:LEU282 4.4 59.4 1.0 CA B:LEU283 4.4 54.9 1.0 N B:LEU283 4.4 57.0 1.0 CA B:SER231 4.5 53.7 1.0 CA B:SER278 4.5 53.8 1.0 OG B:SER284 4.5 49.9 1.0 CG B:GLN232 4.6 49.5 1.0 CB B:TYR281 4.6 59.5 1.0 CA B:LEU282 4.7 59.1 1.0 N B:SER284 4.7 51.9 1.0 C B:ASP230 4.8 56.6 1.0 CA B:TYR281 4.9 60.7 1.0 CB B:ASP230 4.9 58.5 1.0 C B:LEU283 4.9 54.0 1.0 CA B:ASP230 5.0 58.8 1.0 N B:GLU280 5.0 57.8 1.0

M.A.Langereis, Q.Zeng, B.A.Heesters, E.G.Huizinga, R.J.De Groot. The Murine Coronavirus Hemagglutinin-Esterase Receptor- Binding Site: A Major Shift in Ligand Specificity Through Modest Changes in Architecture. Plos Pathog. V. 8 02492 2012.
ISSN: ISSN 1553-7366
PubMed: 22291594
DOI: 10.1371/JOURNAL.PPAT.1002492