Zinc in PDB 4a92: Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.

All present enzymatic activity of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.:
3.4.21.98; 3.6.1.15; 3.6.4.13;

The structure of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor., PDB code: 4a92 was solved by N.Schiering, A.D'arcy, O.Simic, J.Eder, P.Raman, D.I.Svergun, U.Bodendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.40 / 2.73
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	91.972, 110.470, 137.227, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 23.1

The structure of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Zinc atom in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. (pdb code 4a92). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor., PDB code: 4a92:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn999 b:55.0 occ:1.00 SG A:CYS99 2.3 52.6 1.0 SG A:CYS97 2.4 42.8 1.0 SG A:CYS145 2.4 38.0 1.0 O A:HOH2040 3.1 37.3 1.0 CB A:CYS145 3.2 33.5 1.0 CB A:CYS99 3.4 48.6 1.0 CB A:CYS97 3.4 38.1 1.0 N A:CYS99 3.6 47.4 1.0 CA A:CYS97 3.9 38.1 1.0 N A:THR98 3.9 44.4 1.0 CA A:CYS99 4.0 47.8 1.0 OG A:SER147 4.1 52.8 1.0 CB A:SER147 4.2 39.5 1.0 ND1 A:HIS149 4.3 35.6 1.0 C A:CYS97 4.3 45.0 1.0 CB A:HIS149 4.4 29.0 1.0 C A:THR98 4.6 51.5 1.0 CA A:CYS145 4.7 32.2 1.0 N A:GLY100 4.8 47.9 1.0 C A:CYS99 4.8 50.6 1.0 CG A:HIS149 4.8 33.3 1.0 N A:SER147 4.8 35.7 1.0 CA A:THR98 4.9 45.6 1.0

Zinc binding site 2 out of 2 in the Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Full-Length Hcv NS3-4A Protease-Helicase in Complex with A Macrocyclic Protease Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn999 b:0.5 occ:1.00 SG B:CYS145 2.6 95.6 1.0 SG B:CYS99 2.8 0.8 1.0 SG B:CYS97 2.9 0.4 1.0 ND1 B:HIS149 3.4 0.6 1.0 CB B:CYS99 3.6 0.5 1.0 CB B:CYS97 3.7 0.8 1.0 N B:CYS99 3.7 0.7 1.0 CB B:SER147 3.8 0.3 1.0 CB B:CYS145 3.8 90.8 1.0 N B:THR98 3.8 0.5 1.0 OG B:SER147 3.9 0.5 1.0 CA B:CYS97 3.9 0.9 1.0 CB B:HIS149 3.9 0.0 1.0 CG B:HIS149 4.1 0.2 1.0 CA B:CYS99 4.2 0.2 1.0 C B:CYS97 4.3 0.1 1.0 CE1 B:HIS149 4.5 0.2 1.0 C B:THR98 4.8 0.8 1.0 CA B:SER147 4.8 0.2 1.0 N B:SER147 4.8 0.3 1.0 CA B:THR98 4.8 0.2 1.0 OG1 B:THR98 4.8 0.8 1.0 N B:HIS149 4.9 99.8 1.0 CA B:HIS149 5.0 99.8 1.0 O B:HOH2013 5.0 56.1 1.0

N.Schiering, A.D'arcy, F.Villard, O.Simic, M.Kamke, G.Monnet, U.Hassiepen, D.I.Svergun, R.Pulfer, J.Eder, P.Raman, U.Bodendorf. A Macrocyclic Hcv NS3/4A Protease Inhibitor Interacts with Protease and Helicase Residues in the Complex with Its Full- Length Target. Proc.Natl.Acad.Sci.Usa V. 108 21052 2011.
ISSN: ISSN 0027-8424
PubMed: 22160684
DOI: 10.1073/PNAS.1110534108