Crystal structure of the hepatitis C virus NS3 protease in complex with a peptidomimetic inhibitor

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 49% strand (DSSP).

Ligands and binding sites

• DN1 · 3-({(2S)-2-[({(1R)-1-[({(1R)-1-[(R)-carboxy(hydroxy)methyl]-3,3-difluoropropyl}amino)carbonyl]-3-methylbutyl}amino)carb onyl]-2,3-dihydro-1H-indol-2-yl}methyl)thiophene-2-carboxylic acid · ligand · chains A
• DN2 · 3-({(2S)-2-[({(1S)-1-[({(1S)-1-[(R)-carboxy(hydroxy)methyl]-3,3-difluoropropyl}amino)carbonyl]-3-methylbutyl}amino)carbonyl]-2,3-dihydro-1H-indol-2-yl}methyl)thiophene-2-carboxylic acid · ligand · chains B

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

Interfaces

3 interfaces between chains.

• A–C · 1210 Ų buried · 32 hydrogen bonds · protein-protein
• B–D · 1198 Ų buried · 27 hydrogen bonds · protein-protein
• A–B · 382 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 1W3C · Crystal structure of the Hepatitis C Virus NS3 Protease in complex with a peptidomimetic… · 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 Q81755
• Elsewhere: RCSB PDB 1W3C · PDBe 1W3C · UniProt Q81755