Zinc in PDB 2f9v: Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines

The structure of Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines, PDB code: 2f9v was solved by S.L.Bogen, S.Ruan, R.Liu, S.Agrawal, J.Pichardo, A.Prongay, B.Baroudy, A.Saksena, V.Girijavallabhan, F.G.Njoroge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	2.69 / 2.60
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	222.811, 222.811, 75.266, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 26.4

The binding sites of Zinc atom in the Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines (pdb code 2f9v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines, PDB code: 2f9v:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:51.9 occ:1.00 O A:HOH1003 1.6 17.1 1.0 SG A:CYS97 2.2 35.8 1.0 SG A:CYS145 2.2 41.6 1.0 SG A:CYS99 2.4 54.8 1.0 CB A:CYS99 3.3 57.2 1.0 CB A:CYS145 3.4 37.0 1.0 CB A:CYS97 3.5 39.9 1.0 N A:CYS99 3.6 58.1 1.0 N A:THR98 3.7 51.2 1.0 CA A:CYS97 3.8 41.1 1.0 CA A:CYS99 4.0 58.0 1.0 C A:CYS97 4.3 47.1 1.0 CB A:HIS149 4.4 28.2 1.0 C A:THR98 4.4 58.2 1.0 CA A:THR98 4.7 56.6 1.0 CG A:HIS149 4.7 39.7 1.0 C A:CYS99 4.8 59.2 1.0 CA A:CYS145 4.8 35.8 1.0 N A:GLY100 4.9 58.4 1.0 CB A:ALA147 4.9 31.3 1.0

Zinc binding site 2 out of 2 in the Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Hcv NS3 Protease Domain with NS4A Peptide and A Ketoamide Inhibitor with P1 and P2 Cyclopropylalannines within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn902 b:46.2 occ:1.00 O C:HOH903 1.8 18.5 1.0 SG C:CYS145 2.0 33.4 1.0 SG C:CYS97 2.1 29.4 1.0 SG C:CYS99 2.1 42.9 1.0 CB C:CYS145 3.3 32.7 1.0 CB C:CYS99 3.4 41.5 1.0 CB C:CYS97 3.4 34.2 1.0 N C:CYS99 3.6 44.8 1.0 CA C:CYS97 3.8 38.0 1.0 N C:THR98 3.9 49.5 1.0 CA C:CYS99 4.0 43.3 1.0 CB C:HIS149 4.2 30.9 1.0 C C:CYS97 4.3 44.0 1.0 CB C:ALA147 4.5 31.8 1.0 CG C:HIS149 4.6 33.6 1.0 C C:CYS99 4.6 46.0 1.0 C C:THR98 4.7 48.5 1.0 CA C:CYS145 4.7 31.5 1.0 CD2 C:HIS149 4.8 36.9 1.0 N C:GLY100 4.8 48.3 1.0 CA C:THR98 4.9 49.5 1.0

S.L.Bogen, S.Ruan, R.Liu, S.Agrawal, J.Pichardo, A.Prongay, B.Baroudy, A.Saksena, V.Girijavallabhan, F.G.Njoroge. Depeptidization Efforts on P3-P2 A-Ketoamide Inhibitors of Hcv NS3-4A Serine Protease: Effect on Hcv Replicon Activity. Bioorg.Med.Chem.Lett. V. 16 1621 2006.
ISSN: ISSN 0960-894X
PubMed: 16387495
DOI: 10.1016/J.BMCL.2005.12.013