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

The structure of Crystal Structure of NS3/4A Protease in Complex with Mk-5172, PDB code: 3sud 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)	36.48 / 1.96
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.133, 102.698, 73.289, 90.00, 112.54, 90.00
R / Rfree (%)	18.4 / 23.7

The binding sites of Zinc atom in the Crystal Structure of NS3/4A Protease in Complex with Mk-5172 (pdb code 3sud). 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 in Complex with Mk-5172, PDB code: 3sud:
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 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 in Complex with Mk-5172 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1203 b:18.4 occ:1.00 SG A:CYS1097 1.7 26.4 1.0 SG A:CYS1145 2.2 19.8 1.0 SG A:CYS1099 2.8 40.7 1.0 CB A:CYS1099 2.9 35.3 1.0 CB A:CYS1145 2.9 21.1 1.0 CB A:CYS1097 3.2 25.7 1.0 N A:CYS1099 3.5 33.0 1.0 ND1 A:HIS1149 3.6 27.3 1.0 CA A:CYS1097 3.7 25.7 1.0 CA A:CYS1099 3.8 34.5 1.0 N A:THR1098 4.0 28.1 1.0 CB A:HIS1149 4.1 22.9 1.0 CG A:HIS1149 4.2 24.9 1.0 C A:CYS1097 4.3 26.7 1.0 CA A:CYS1145 4.4 21.3 1.0 CB A:ALA1147 4.6 23.7 1.0 CE1 A:HIS1149 4.6 28.2 1.0 N A:GLY1100 4.7 33.4 1.0 C A:THR1098 4.7 31.7 1.0 C A:CYS1099 4.7 33.9 1.0 CD A:PRO1146 4.9 25.1 1.0 N A:ALA1147 5.0 23.0 1.0 CA A:THR1098 5.0 29.8 1.0 C A:CYS1145 5.0 22.2 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of NS3/4A Protease 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 in Complex with Mk-5172 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1202 b:20.6 occ:1.00 SG B:CYS1145 2.2 19.3 1.0 SG B:CYS1099 2.2 33.6 1.0 SG B:CYS1097 2.3 25.8 1.0 CB B:CYS1145 2.9 21.6 1.0 CB B:CYS1099 3.2 32.9 1.0 CB B:CYS1097 3.5 24.6 1.0 N B:CYS1099 3.7 32.6 1.0 CA B:CYS1097 3.9 24.2 1.0 CA B:CYS1099 4.0 33.0 1.0 N B:THR1098 4.1 31.1 1.0 CB B:HIS1149 4.3 27.5 1.0 ND1 B:HIS1149 4.3 31.9 1.0 CA B:CYS1145 4.3 22.0 1.0 C B:CYS1097 4.4 24.4 1.0 CB B:ALA1147 4.5 29.2 1.0 CD B:PRO1146 4.6 24.6 1.0 CG B:HIS1149 4.6 29.4 1.0 C B:CYS1099 4.7 33.3 1.0 N B:GLY1100 4.8 33.0 1.0 N B:ALA1147 4.8 27.4 1.0 C B:THR1098 4.8 32.5 1.0 C B:CYS1145 4.9 22.6 1.0 CB B:SER1101 4.9 32.7 1.0 N B:PRO1146 5.0 23.9 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of NS3/4A Protease 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 in Complex with Mk-5172 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1202 b:26.1 occ:1.00 SG C:CYS1097 2.1 33.4 1.0 SG C:CYS1145 2.3 27.2 1.0 SG C:CYS1099 3.0 53.1 1.0 CB C:CYS1099 3.0 48.1 1.0 CB C:CYS1145 3.1 27.6 1.0 CB C:CYS1097 3.2 32.7 1.0 N C:CYS1099 3.7 42.0 1.0 CA C:CYS1097 3.7 33.1 1.0 CA C:CYS1099 4.0 45.8 1.0 N C:THR1098 4.1 35.0 1.0 C C:CYS1097 4.2 34.2 1.0 ND1 C:HIS1149 4.2 28.9 1.0 CB C:HIS1149 4.4 27.0 1.0 N C:GLY1100 4.6 45.3 1.0 CA C:CYS1145 4.6 27.0 1.0 CB C:ALA1147 4.6 28.8 1.0 CG C:HIS1149 4.6 28.1 1.0 C C:CYS1099 4.8 46.2 1.0 CB C:SER1101 4.8 42.2 1.0 C C:THR1098 4.8 39.1 1.0 N C:SER1101 4.9 43.3 1.0 CD C:PRO1146 4.9 28.9 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of NS3/4A Protease 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 in Complex with Mk-5172 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1202 b:21.8 occ:1.00 SG D:CYS1145 2.0 23.6 1.0 SG D:CYS1099 2.3 30.5 1.0 ND1 D:HIS1149 2.3 26.3 1.0 SG D:CYS1097 2.3 28.8 1.0 CG D:HIS1149 3.2 25.7 1.0 CB D:CYS1145 3.2 23.2 1.0 CB D:HIS1149 3.3 24.5 1.0 CE1 D:HIS1149 3.4 26.8 1.0 CB D:CYS1097 3.4 29.4 1.0 CB D:CYS1099 3.5 32.5 1.0 CA D:CYS1097 3.8 30.5 1.0 N D:CYS1099 3.9 34.4 1.0 N D:THR1098 4.0 33.0 1.0 CB D:ALA1147 4.1 25.2 1.0 CA D:CYS1099 4.3 33.9 1.0 O D:HOH1319 4.4 29.8 1.0 C D:CYS1097 4.4 32.2 1.0 CD2 D:HIS1149 4.4 26.1 1.0 NE2 D:HIS1149 4.4 27.4 1.0 N D:HIS1149 4.5 23.4 1.0 CA D:HIS1149 4.5 23.6 1.0 CA D:CYS1145 4.6 22.5 1.0 N D:ALA1147 4.9 24.4 1.0 C D:THR1098 4.9 35.1 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