Sodium in PDB 4i32: Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4

All present enzymatic activity of Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4:
2.7.7.48; 3.4.21.98; 3.6.1.15; 3.6.4.13;

The structure of Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4, PDB code: 4i32 was solved by C.T.Lemke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.84 / 2.30
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	93.671, 93.671, 81.830, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 24.8

The binding sites of Sodium atom in the Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4 (pdb code 4i32). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4, PDB code: 4i32:

Sodium binding site 1 out of 1 in the Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Hcv NS3/4A D168V Protease Complexed with Compound 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na201 b:63.3 occ:1.00 O A:ALA111 2.7 51.8 1.0 O A:HOH312 2.8 48.7 1.0 O A:HOH336 2.9 56.7 1.0 O A:HOH337 3.1 57.8 1.0 O A:ALA5 3.2 45.9 1.0 C A:ALA111 3.6 50.0 1.0 OD1 A:ASP112 3.8 58.0 1.0 O A:HOH318 3.8 52.2 1.0 CA A:ASP112 4.1 50.3 1.0 N A:ASP112 4.2 48.4 1.0 C A:ALA5 4.3 44.0 1.0 CB A:ALA111 4.4 44.5 1.0 CA A:ALA111 4.7 47.8 1.0 N A:ALA5 4.7 46.5 1.0 CG A:ASP112 4.8 54.9 1.0 O A:HIS110 4.8 53.6 1.0 O A:HOH313 4.9 49.1 1.0 CA A:ALA5 5.0 48.8 1.0

J.A.O'meara, C.T.Lemke, C.Godbout, G.Kukolj, L.Lagace, B.Moreau, D.Thibeault, P.W.White, M.Llinas-Brunet. Molecular Mechanism By Which A Potent Hepatitis C Virus NS3-NS4A Protease Inhibitor Overcomes Emergence of Resistance. J.Biol.Chem. V. 288 5673 2013.
ISSN: ISSN 0021-9258
PubMed: 23271737
DOI: 10.1074/JBC.M112.439455