Zinc in PDB 2a4r: Hcv NS3 Protease Domain with A Ketoamide Inhibitor Covalently Bound.

The structure of Hcv NS3 Protease Domain with A Ketoamide Inhibitor Covalently Bound., PDB code: 2a4r was solved by S.Bogen, A.K.Saksena, A.Arasappan, H.Gu, F.G.Njoroge, V.Girijavallabhan, J.Pichardo, N.Butkiewicz, A.Prongay, V.Madison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.40
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	223.603, 223.603, 75.354, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 27.1

The binding sites of Zinc atom in the Hcv NS3 Protease Domain with A Ketoamide Inhibitor Covalently Bound. (pdb code 2a4r). 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 A Ketoamide Inhibitor Covalently Bound., PDB code: 2a4r:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Hcv NS3 Protease Domain with A Ketoamide Inhibitor Covalently Bound.


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 A Ketoamide Inhibitor Covalently Bound. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:46.8 occ:1.00 O A:HOH405 2.0 20.1 1.0 SG A:CYS97 2.2 42.5 1.0 SG A:CYS145 2.3 42.6 1.0 SG A:CYS99 2.4 60.4 1.0 CB A:CYS145 3.4 37.6 1.0 CB A:CYS97 3.4 45.2 1.0 CB A:CYS99 3.5 60.1 1.0 N A:THR98 3.7 55.9 1.0 CA A:CYS97 3.8 46.3 1.0 N A:CYS99 3.8 61.7 1.0 C A:CYS97 4.2 51.4 1.0 CA A:CYS99 4.2 61.2 1.0 CB A:HIS149 4.3 34.6 1.0 CB A:ALA147 4.3 41.9 1.0 C A:THR98 4.4 61.8 1.0 CG A:HIS149 4.6 38.3 1.0 CA A:THR98 4.7 59.8 1.0 CA A:CYS145 4.8 36.9 1.0 C A:CYS99 4.9 61.4 1.0 N A:ALA147 4.9 39.5 1.0 CD2 A:HIS149 5.0 42.5 1.0

Zinc binding site 2 out of 2 in the Hcv NS3 Protease Domain with A Ketoamide Inhibitor Covalently Bound.


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 A Ketoamide Inhibitor Covalently Bound. within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn302 b:42.9 occ:1.00 O C:HOH304 2.1 13.2 1.0 SG C:CYS145 2.1 37.2 1.0 SG C:CYS97 2.2 40.0 1.0 SG C:CYS99 2.2 46.8 1.0 CB C:CYS145 3.3 34.0 1.0 CB C:CYS99 3.4 44.5 1.0 CB C:CYS97 3.5 39.1 1.0 N C:CYS99 3.6 46.4 1.0 CA C:CYS97 3.8 41.0 1.0 N C:THR98 3.9 44.6 1.0 CA C:CYS99 4.0 46.5 1.0 C C:CYS97 4.3 42.4 1.0 CB C:HIS149 4.3 28.4 1.0 CB C:ALA147 4.5 29.0 1.0 C C:CYS99 4.6 48.4 1.0 C C:THR98 4.6 46.5 1.0 N C:GLY100 4.7 49.9 1.0 CA C:CYS145 4.7 31.8 1.0 CG C:HIS149 4.8 29.4 1.0 CA C:THR98 4.9 45.7 1.0 N C:ALA147 4.9 34.4 1.0 ND1 C:HIS149 4.9 33.0 1.0

S.Bogen, A.K.Saksena, A.Arasappan, H.Gu, F.G.Njoroge, V.Girijavallabhan, J.Pichardo, N.Butkiewicz, A.Prongay, V.Madison. Hepatitis C Virus NS3-4A Serine Protease Inhibitors: Use of A P2-P1 Cyclopropyl Alanine Combination For Improved Potency. Bioorg.Med.Chem.Lett. V. 15 4515 2005.
ISSN: ISSN 0960-894X
PubMed: 16112862
DOI: 10.1016/J.BMCL.2005.07.009