Zinc in PDB 3kf2: The Hcv NS3/NS4A Protease Apo Structure

All present enzymatic activity of The Hcv NS3/NS4A Protease Apo Structure:
3.4.21.98;

The structure of The Hcv NS3/NS4A Protease Apo Structure, PDB code: 3kf2 was solved by J.D.Lindberg, S.Nystrom, M.D.Cummings, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	112.46 / 2.50
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	224.924, 224.924, 75.545, 90.00, 90.00, 120.00
R / Rfree (%)	20.5 / 23.5

The binding sites of Zinc atom in the The Hcv NS3/NS4A Protease Apo Structure (pdb code 3kf2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Hcv NS3/NS4A Protease Apo Structure, PDB code: 3kf2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Hcv NS3/NS4A Protease Apo Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Hcv NS3/NS4A Protease Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:31.0 occ:1.00 SG A:CYS145 2.3 27.4 1.0 SG A:CYS97 2.3 30.6 1.0 O A:HOH190 2.3 9.9 1.0 SG A:CYS99 2.4 39.3 1.0 CB A:CYS145 3.1 25.8 1.0 CB A:CYS99 3.5 38.5 1.0 CB A:CYS97 3.5 31.8 1.0 N A:CYS99 3.8 37.8 1.0 CA A:CYS97 3.9 32.2 1.0 N A:THR98 4.1 34.5 1.0 CA A:CYS99 4.1 38.5 1.0 CB A:HIS149 4.3 22.9 1.0 C A:CYS97 4.4 33.1 1.0 O A:CYS99 4.4 40.0 1.0 C A:CYS99 4.4 38.9 1.0 CB A:ALA147 4.5 25.0 1.0 CA A:CYS145 4.5 25.9 1.0 CD2 A:HIS149 4.7 25.0 1.0 CG A:HIS149 4.7 23.9 1.0 CD A:PRO146 4.8 26.3 1.0 C A:THR98 4.9 37.1 1.0 N A:ALA147 4.9 26.2 1.0

Zinc binding site 2 out of 2 in the The Hcv NS3/NS4A Protease Apo Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Hcv NS3/NS4A Protease Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn902 b:38.7 occ:1.00 SG B:CYS97 2.2 34.8 1.0 O B:HOH190 2.3 8.5 1.0 SG B:CYS145 2.4 32.0 1.0 SG B:CYS99 2.5 43.6 1.0 CB B:CYS145 3.1 29.0 1.0 CB B:CYS99 3.3 43.2 1.0 CB B:CYS97 3.4 36.0 1.0 N B:CYS99 3.7 43.0 1.0 CA B:CYS97 3.8 36.4 1.0 CA B:CYS99 4.0 43.2 1.0 N B:THR98 4.0 39.2 1.0 C B:CYS97 4.3 37.4 1.0 C B:CYS99 4.4 43.4 1.0 O B:CYS99 4.4 44.0 1.0 CB B:HIS149 4.5 32.5 1.0 CA B:CYS145 4.6 29.0 1.0 C B:THR98 4.8 42.4 1.0 CB B:ALA147 4.8 30.7 1.0

M.D.Cummings, J.D.Lindberg, T.-I.Lin, H.De Kock, O.Lenz, E.Lilja, S.Fellander, V.Baraznenok, S.Nystrom, M.Nilsson, L.Vrang, M.Edlund, A.Rosenquist, B.Samuelsson, P.Raboisson, K.Simmen. Induced-Fit Binding of the Macrocyclic Noncovalent Inhibitor TMC435 to Its Hcv NS3/NS4A Protease Target Angew.Chem.Int.Ed.Engl. V. 49 1652 2010.
ISSN: ISSN 1433-7851
PubMed: 20166108
DOI: 10.1002/ANIE.200906696