Zinc in PDB 4k8b: Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor

All present enzymatic activity of Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor:
3.4.21.98;

The structure of Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor, PDB code: 4k8b was solved by H.Nar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.93 / 2.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	76.182, 76.182, 169.206, 90.00, 90.00, 120.00
R / Rfree (%)	20.3 / 23.2

The binding sites of Zinc atom in the Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor (pdb code 4k8b). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor, PDB code: 4k8b:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor


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 Hcv NS3/4A Protease Complexed with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:83.4 occ:1.00 SG A:CYS99 2.2 87.2 1.0 SG A:CYS97 2.2 78.5 1.0 SG A:CYS145 2.6 78.2 1.0 CB A:CYS99 2.7 82.9 1.0 O A:HOH306 3.0 32.2 1.0 CB A:CYS145 3.1 73.4 1.0 CB A:CYS97 3.1 71.6 1.0 N A:CYS99 3.3 80.7 1.0 CA A:CYS99 3.6 83.6 1.0 CA A:CYS97 3.6 72.7 1.0 N A:THR98 3.7 76.4 1.0 C A:CYS97 4.0 79.4 1.0 CB A:HIS149 4.1 63.9 1.0 C A:THR98 4.4 82.0 1.0 ND1 A:HIS149 4.4 73.3 1.0 CA A:CYS145 4.6 71.0 1.0 CA A:THR98 4.6 78.0 1.0 C A:CYS99 4.7 87.2 1.0 CG A:HIS149 4.7 68.9 1.0 N A:GLY100 4.7 80.8 1.0 CB A:SER147 4.9 76.5 1.0 N A:CYS97 4.9 70.8 1.0 OG A:SER147 4.9 88.8 1.0 O A:HIS149 5.0 59.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Hcv NS3/4A Protease Complexed with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:94.8 occ:1.00 SG B:CYS97 2.2 86.7 1.0 SG B:CYS99 2.2 91.7 1.0 SG B:CYS145 2.6 77.5 1.0 CB B:CYS99 2.7 88.0 1.0 O B:HOH325 2.9 52.4 1.0 CB B:CYS145 3.1 72.4 1.0 CB B:CYS97 3.1 79.5 1.0 N B:CYS99 3.2 89.1 1.0 CA B:CYS99 3.5 90.1 1.0 CA B:CYS97 3.6 81.2 1.0 N B:THR98 3.6 87.1 1.0 C B:CYS97 4.0 88.6 1.0 CB B:HIS149 4.1 75.8 1.0 O B:HOH323 4.2 41.5 1.0 C B:THR98 4.3 94.5 1.0 CA B:THR98 4.6 89.7 1.0 CA B:CYS145 4.6 70.3 1.0 C B:CYS99 4.7 91.9 1.0 CG B:HIS149 4.7 82.3 1.0 N B:GLY100 4.7 83.3 1.0 CD2 B:HIS149 4.7 86.8 1.0 N B:CYS97 4.9 79.0 1.0 CB B:SER147 4.9 84.4 1.0 OG B:SER147 5.0 96.2 1.0 O B:HIS149 5.0 72.6 1.0

S.R.Laplante, H.Nar, C.T.Lemke, A.Jakalian, N.Aubry, S.H.Kawai. Ligand Bioactive Conformation Plays A Critical Role in the Design of Drugs That Target the Hepatitis C Virus NS3 Protease. J.Med.Chem. V. 57 1777 2014.
ISSN: ISSN 0022-2623
PubMed: 24144444
DOI: 10.1021/JM401338C