Zinc in PDB 3suf: Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172

The structure of Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172, PDB code: 3suf was solved by C.A.Schiffer, K.P.Romano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.22 / 2.19
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.004, 103.560, 73.510, 90.00, 112.04, 90.00
R / Rfree (%)	19.9 / 25.9

The binding sites of Zinc atom in the Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172 (pdb code 3suf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172, PDB code: 3suf:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172


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 NS3/4A Protease Variant D168A in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1202 b:36.7 occ:1.00 SG A:CYS1097 2.2 26.6 1.0 SG A:CYS1099 2.5 27.4 1.0 SG A:CYS1145 2.8 23.9 1.0 CB A:CYS1097 3.3 27.7 1.0 CB A:CYS1099 3.3 26.9 1.0 CB A:CYS1145 3.3 24.5 1.0 N A:CYS1099 3.5 27.1 1.0 ND1 A:HIS1149 3.5 31.9 1.0 CA A:CYS1097 3.7 28.1 1.0 N A:THR1098 4.0 27.8 1.0 CA A:CYS1099 4.0 27.6 1.0 CB A:HIS1149 4.0 31.1 1.0 CG A:HIS1149 4.2 31.1 1.0 C A:CYS1097 4.2 28.9 1.0 CE1 A:HIS1149 4.5 32.4 1.0 C A:THR1098 4.6 26.9 1.0 C A:CYS1099 4.6 28.1 1.0 N A:GLY1100 4.7 28.7 1.0 CA A:CYS1145 4.8 22.9 1.0 CA A:THR1098 4.9 27.9 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172


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 NS3/4A Protease Variant D168A in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1203 b:36.6 occ:1.00 SG B:CYS1145 1.8 28.5 1.0 SG B:CYS1097 2.1 32.8 1.0 SG B:CYS1099 2.4 43.5 1.0 CB B:CYS1145 2.7 28.6 1.0 CB B:CYS1097 3.3 34.3 1.0 ND1 B:HIS1149 3.5 34.5 1.0 CB B:CYS1099 3.5 40.2 1.0 CA B:CYS1097 4.0 34.3 1.0 N B:CYS1099 4.1 37.8 1.0 CA B:CYS1145 4.2 28.8 1.0 CG B:HIS1149 4.3 33.9 1.0 CE1 B:HIS1149 4.3 35.0 1.0 CB B:HIS1149 4.3 32.3 1.0 CA B:CYS1099 4.4 39.3 1.0 N B:THR1098 4.4 36.7 1.0 CB B:ALA1147 4.4 30.1 1.0 CD B:PRO1146 4.5 31.0 1.0 N B:ALA1147 4.6 30.8 1.0 C B:CYS1097 4.6 35.9 1.0 C B:CYS1145 4.6 28.5 1.0 N B:PRO1146 4.7 31.3 1.0 N B:GLY1100 4.8 37.7 1.0 CB B:SER1101 4.9 41.2 1.0 N B:CYS1145 5.0 27.5 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1202 b:47.3 occ:1.00 SG C:CYS1099 1.6 43.5 1.0 SG C:CYS1097 2.3 34.7 1.0 CB C:CYS1099 2.7 41.9 1.0 SG C:CYS1145 2.8 41.0 1.0 CB C:CYS1145 3.2 40.2 1.0 N C:CYS1099 3.3 41.3 1.0 CA C:CYS1099 3.5 42.2 1.0 CB C:CYS1097 3.6 33.3 1.0 N C:THR1098 4.0 34.8 1.0 CA C:CYS1097 4.0 32.9 1.0 ND1 C:HIS1149 4.2 37.1 1.0 C C:CYS1099 4.2 43.7 1.0 C C:CYS1097 4.4 34.7 1.0 N C:GLY1100 4.4 45.2 1.0 C C:THR1098 4.5 38.4 1.0 CB C:HIS1149 4.6 36.2 1.0 CA C:CYS1145 4.7 39.1 1.0 CB C:ALA1147 4.7 37.3 1.0 CG C:HIS1149 4.9 35.9 1.0 CA C:THR1098 4.9 37.3 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of NS3/4A Protease Variant D168A in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1202 b:33.1 occ:1.00 SG D:CYS1145 2.1 29.7 1.0 SG D:CYS1097 2.2 33.3 1.0 SG D:CYS1099 2.5 42.4 1.0 ND1 D:HIS1149 2.8 35.5 1.0 CG D:HIS1149 3.1 35.9 1.0 CB D:CYS1145 3.2 30.0 1.0 CB D:HIS1149 3.3 33.6 1.0 CB D:CYS1097 3.6 40.5 1.0 CE1 D:HIS1149 3.6 34.2 1.0 CB D:CYS1099 3.7 41.5 1.0 CA D:CYS1097 4.0 41.8 1.0 CD2 D:HIS1149 4.0 36.1 1.0 CB D:ALA1147 4.2 30.9 1.0 N D:THR1098 4.2 42.9 1.0 NE2 D:HIS1149 4.3 36.0 1.0 N D:CYS1099 4.3 42.4 1.0 N D:HIS1149 4.4 32.3 1.0 CA D:HIS1149 4.4 33.3 1.0 CA D:CYS1145 4.6 30.2 1.0 CA D:CYS1099 4.6 43.1 1.0 C D:CYS1097 4.7 43.2 1.0 N D:ALA1147 4.9 31.6 1.0 CA D:ALA1147 5.0 31.7 1.0

K.P.Romano, A.Ali, C.Aydin, D.Soumana, A.Ozen, L.M.Deveau, C.Silver, H.Cao, A.Newton, C.J.Petropoulos, W.Huang, C.A.Schiffer. The Molecular Basis of Drug Resistance Against Hepatitis C Virus NS3/4A Protease Inhibitors. Plos Pathog. V. 8 02832 2012.
ISSN: ISSN 1553-7366
PubMed: 22910833
DOI: 10.1371/JOURNAL.PPAT.1002832