Zinc in PDB 4h9k: Crystal Structure of Cleavage Site Mutant of Npro of Classical Swine Fever Virus.

The structure of Crystal Structure of Cleavage Site Mutant of Npro of Classical Swine Fever Virus., PDB code: 4h9k was solved by K.Gottipati, N.Ruggli, M.Gerber, J-D.Tratschin, M.Benning, H.Bellamy, K.H.Choi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.70 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.489, 58.298, 75.464, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 21.6

The binding sites of Zinc atom in the Crystal Structure of Cleavage Site Mutant of Npro of Classical Swine Fever Virus. (pdb code 4h9k). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Cleavage Site Mutant of Npro of Classical Swine Fever Virus., PDB code: 4h9k:

Zinc binding site 1 out of 1 in the Crystal Structure of Cleavage Site Mutant of Npro of Classical Swine Fever Virus.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Cleavage Site Mutant of Npro of Classical Swine Fever Virus. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn204 b:10.3 occ:1.00 OXT A:ALA168 1.9 9.0 1.0 NE2 A:HIS49 2.1 9.6 1.0 SG A:CYS69 2.3 10.2 1.0 C A:ALA168 2.9 12.2 1.0 CE1 A:HIS49 3.0 10.7 1.0 CD2 A:HIS49 3.1 10.9 1.0 O A:ALA168 3.2 12.0 1.0 CB A:CYS69 3.3 10.2 1.0 O A:HOH348 3.5 16.6 1.0 ND1 A:HIS49 4.2 10.2 1.0 CG A:HIS49 4.2 8.7 1.0 CA A:ALA168 4.3 9.4 1.0 N A:ALA168 4.4 7.6 1.0 CA A:CYS69 4.6 10.0 1.0 O A:HOH434 4.6 22.6 1.0 O A:HOH326 4.6 18.5 1.0 C A:SER167 4.8 8.3 1.0 N A:CYS69 4.8 9.0 1.0

K.Gottipati, N.Ruggli, M.Gerber, J.D.Tratschin, M.Benning, H.Bellamy, K.H.Choi. The Structure of Classical Swine Fever Virus N(Pro): A Novel Cysteine Autoprotease and Zinc-Binding Protein Involved in Subversion of Type I Interferon Induction. Plos Pathog. V. 9 03704 2013.
ISSN: ISSN 1553-7366
PubMed: 24146623
DOI: 10.1371/JOURNAL.PPAT.1003704