Crystal structure of HCV NS3/4A protease A156T variant in complex with 5172-linear (mk-5172 linear analogue)

Structure

x-ray diffraction · 4 distinct chains · 15% helix, 45% strand (DSSP).

Ligands and binding sites

• 5RS · ~{tert}-butyl ~{N}-[(2~{S})-1-[(2~{S},4~{R})-2-[[(1~{R},2~{R})-1-(cyclopropylsulfonylcarbamoyl)-2-ethyl-cyclopropyl]carbamoyl]-4-(3-ethyl-7-methoxy-quinoxalin-2-yl)oxy-pyrrolidin-1-yl]-3,3-dimethyl-1-oxidanylidene-butan-2-yl]carbamate · ligand · 4 copies · chains A, C, B, D
• ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
• CL · Chloride ion · ion · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• A–C · 333 Ų buried · 3 hydrogen bonds · protein-protein
• B–D · 192 Ų buried · 2 hydrogen bonds · protein-protein
• B–C · 182 Ų buried · 0 hydrogen bonds · protein-protein
• A–D · 152 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 5ETX · Crystal structure of HCV NS3/4A protease A156T variant in complex with 5172-Linear… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt C1KIK8
• Elsewhere: RCSB PDB 5ETX · PDBe 5ETX · UniProt C1KIK8