Zinc in PDB 3sue: Crystal Structure of NS3/4A Protease Variant R155K in Complex with Mk- 5172

The structure of Crystal Structure of NS3/4A Protease Variant R155K in Complex with Mk- 5172, PDB code: 3sue 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)	32.24 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.335, 103.324, 73.498, 90.00, 112.58, 90.00
R / Rfree (%)	18.6 / 22.9

The binding sites of Zinc atom in the Crystal Structure of NS3/4A Protease Variant R155K in Complex with Mk- 5172 (pdb code 3sue). 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 R155K in Complex with Mk- 5172, PDB code: 3sue:
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 R155K 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 R155K in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1202 b:33.4 occ:1.00 SG A:CYS1097 2.2 38.8 1.0 SG A:CYS1145 2.3 45.8 1.0 SG A:CYS1099 2.7 57.2 1.0 CB A:CYS1099 2.8 54.7 1.0 CB A:CYS1145 3.1 42.7 1.0 CB A:CYS1097 3.3 36.9 1.0 N A:CYS1099 3.4 49.3 1.0 ND1 A:HIS1149 3.5 50.7 1.0 CA A:CYS1097 3.7 36.9 1.0 CA A:CYS1099 3.7 53.0 1.0 N A:THR1098 3.8 41.4 1.0 C A:CYS1097 4.1 38.4 1.0 CB A:HIS1149 4.2 45.4 1.0 CG A:HIS1149 4.3 48.9 1.0 C A:THR1098 4.5 47.0 1.0 CE1 A:HIS1149 4.5 53.7 1.0 CB A:ALA1147 4.6 53.1 1.0 CA A:CYS1145 4.6 40.4 1.0 C A:CYS1099 4.6 53.9 1.0 CA A:THR1098 4.7 43.5 1.0 N A:GLY1100 4.8 52.2 1.0 N A:ALA1147 5.0 48.5 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of NS3/4A Protease Variant R155K 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 R155K 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:CYS1097 2.0 28.8 1.0 SG B:CYS1145 2.5 23.2 1.0 SG B:CYS1099 2.6 33.0 1.0 CB B:CYS1097 3.0 28.0 1.0 CB B:CYS1145 3.0 22.6 1.0 CB B:CYS1099 3.5 34.8 1.0 CA B:CYS1097 3.5 28.6 1.0 N B:CYS1099 3.7 32.7 1.0 N B:THR1098 4.1 31.1 1.0 C B:CYS1097 4.1 29.7 1.0 CA B:CYS1099 4.2 34.2 1.0 CB B:HIS1149 4.4 25.6 1.0 CA B:CYS1145 4.5 22.8 1.0 CB B:ALA1147 4.5 26.9 1.0 ND1 B:HIS1149 4.6 28.6 1.0 N B:GLY1100 4.6 30.7 1.0 N B:CYS1097 4.8 28.4 1.0 C B:CYS1099 4.8 33.5 1.0 CD B:PRO1146 4.8 25.2 1.0 C B:THR1098 4.9 33.4 1.0 CG B:HIS1149 5.0 27.8 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of NS3/4A Protease Variant R155K 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 R155K in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1202 b:25.6 occ:1.00 SG C:CYS1099 1.8 57.0 1.0 SG C:CYS1097 1.9 41.0 1.0 SG C:CYS1145 2.2 25.8 1.0 CB C:CYS1099 2.6 58.4 1.0 CB C:CYS1145 2.9 25.0 1.0 CB C:CYS1097 3.1 38.8 1.0 CA C:CYS1097 3.7 40.5 1.0 CA C:CYS1099 3.7 57.5 1.0 N C:CYS1099 3.7 53.2 1.0 ND1 C:HIS1149 4.2 30.1 1.0 C C:CYS1097 4.3 42.8 1.0 CA C:CYS1145 4.4 25.0 1.0 N C:GLY1100 4.4 52.1 1.0 C C:CYS1099 4.5 56.6 1.0 N C:THR1098 4.6 47.5 1.0 CB C:HIS1149 4.6 28.5 1.0 CB C:ALA1147 4.6 28.1 1.0 CG C:HIS1149 4.9 30.0 1.0 N C:SER1101 5.0 55.1 1.0 N C:CYS1145 5.0 24.6 1.0 O C:CYS1097 5.0 41.5 1.0 N C:CYS1097 5.0 38.2 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of NS3/4A Protease Variant R155K 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 R155K in Complex with Mk- 5172 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1202 b:24.5 occ:1.00 SG D:CYS1099 1.9 32.8 1.0 SG D:CYS1145 2.2 24.9 1.0 ND1 D:HIS1149 2.3 27.4 1.0 SG D:CYS1097 2.3 25.9 1.0 CB D:CYS1099 3.0 34.6 1.0 CG D:HIS1149 3.1 27.7 1.0 CB D:HIS1149 3.3 26.8 1.0 CB D:CYS1145 3.3 24.1 1.0 CB D:CYS1097 3.3 26.2 1.0 CE1 D:HIS1149 3.3 28.4 1.0 N D:CYS1099 3.7 34.6 1.0 CA D:CYS1097 3.8 27.5 1.0 CA D:CYS1099 3.9 36.1 1.0 N D:THR1098 4.0 31.3 1.0 CD2 D:HIS1149 4.3 29.3 1.0 C D:CYS1097 4.4 30.2 1.0 NE2 D:HIS1149 4.4 29.6 1.0 CA D:HIS1149 4.5 27.0 1.0 CB D:ALA1147 4.5 27.3 1.0 N D:HIS1149 4.6 26.7 1.0 CA D:CYS1145 4.7 23.8 1.0 C D:THR1098 4.8 35.4 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