Zinc in PDB 4ktc: NS3/NS4A Protease with Inhibitor

All present enzymatic activity of NS3/NS4A Protease with Inhibitor:
3.4.21.98; 3.6.1.15; 3.6.4.13;

The structure of NS3/NS4A Protease with Inhibitor, PDB code: 4ktc was solved by H.Zhang, J.Ballard, G.P.A.Vigers, B.J.Brandhuber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.46 / 2.30
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	72.988, 72.988, 127.480, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 25.8

The binding sites of Zinc atom in the NS3/NS4A Protease with Inhibitor (pdb code 4ktc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the NS3/NS4A Protease with Inhibitor, PDB code: 4ktc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the NS3/NS4A Protease with Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of NS3/NS4A Protease with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:66.4 occ:1.00 SG A:CYS99 2.2 62.4 1.0 SG A:CYS97 2.3 50.9 1.0 O A:HOH310 2.3 35.0 1.0 SG A:CYS145 2.4 57.2 1.0 CB A:CYS145 3.1 53.1 1.0 N A:CYS99 3.1 58.1 1.0 CB A:CYS99 3.4 61.5 1.0 N A:THR98 3.4 57.5 1.0 OG A:SER147 3.6 70.1 1.0 CB A:CYS97 3.6 53.5 1.0 CA A:CYS99 3.8 61.2 1.0 CA A:CYS97 4.0 57.5 1.0 C A:THR98 4.1 58.5 1.0 C A:CYS97 4.2 59.1 1.0 CA A:THR98 4.3 58.7 1.0 N A:GLY100 4.3 60.2 1.0 C A:CYS99 4.4 60.5 1.0 CB A:HIS149 4.5 66.7 1.0 CA A:CYS145 4.6 52.0 1.0 CB A:SER147 4.7 63.8 1.0 CG A:HIS149 4.8 75.6 1.0 N A:SER101 4.9 52.3 1.0

Zinc binding site 2 out of 2 in the NS3/NS4A Protease with Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of NS3/NS4A Protease with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:72.7 occ:1.00 SG C:CYS145 2.1 58.4 1.0 SG C:CYS97 2.4 46.5 1.0 CB C:CYS99 2.6 54.9 1.0 SG C:CYS99 2.9 67.1 1.0 N C:CYS99 3.2 57.7 1.0 CB C:CYS145 3.2 53.6 1.0 CA C:CYS99 3.4 56.5 1.0 CB C:CYS97 3.5 49.3 1.0 CA C:CYS97 3.8 48.0 1.0 N C:THR98 3.9 51.8 1.0 CB C:HIS149 4.0 51.9 1.0 C C:CYS97 4.3 50.6 1.0 C C:THR98 4.4 55.8 1.0 CG C:HIS149 4.5 56.5 1.0 C C:CYS99 4.6 55.9 1.0 OG C:SER147 4.7 60.5 1.0 CA C:CYS145 4.7 51.5 1.0 ND1 C:HIS149 4.7 58.0 1.0 CA C:THR98 4.7 57.4 1.0 CB C:SER147 4.8 58.1 1.0 N C:GLY100 4.9 56.1 1.0

Y.Jiang, S.W.Andrews, K.R.Condroski, B.Buckman, V.Serebryany, S.Wenglowsky, A.L.Kennedy, M.R.Madduru, B.Wang, M.Lyon, G.A.Doherty, B.T.Woodard, C.Lemieux, M.G.Do, H.Zhang, J.Ballard, G.Vigers, B.J.Brandhuber, P.Stengel, J.A.Josey, L.Beigelman, L.Blatt, S.D.Seiwert. Discovery of Danoprevir (Itmn-191/R7227), A Highly Selective and Potent Inhibitor of Hepatitis C Virus (Hcv) NS3/4A Protease. J.Med.Chem. V. 57 1753 2014.
ISSN: ISSN 0022-2623
PubMed: 23672640
DOI: 10.1021/JM400164C