EC Number   |
|---|
   3.4.21.98 | 3D structural model threaded through a template crystal structure of HCV-1b NS3 protease. The model protease has rigid structural features. Local dynamics and 4D analysis of the interactions between the catalytic triad residues His57, Asp81, and Ser139 indicate conformational instability of the catalytic site in HCV-4a NS3 protease |
| 3.4.21.98 | crystal structure of a recombinant truncated HCV NS3 protease domain complexed with a synthetic peptide encompassing the essential NS3-binding region of NS4A at 2.5 A resolution |
| 3.4.21.98 | crystal structure of NS2B-NS3pro cocrystallized with the tetrapeptide aldehyde Bz-nKRR-HS1. S2 pockets are the key peptide recognition sites. A residue capable of both pi-stacking and hydrogen bonding is favored in the S1 pocket, while a positively charged residue is preferred in the S2 pocket |
| 3.4.21.98 | crystal structure of NS2B/NS3 protease reveals that Asn-84 of the NS2B cofactor is within hydrogen bonding distance of the P2 Lys of the bound ligand.Asn-84 is located within a highly conserved region of the cofactor, the Gly residue on the N-terminal side is completely conserved, and the third residue on the C-terminal side is a highly conserved hydrophobic Leu or Ile |
| 3.4.21.98 | crystal structure of protease-inhibitor complex |
| 3.4.21.98 | genotype 1a HCV protease domain with R155K mutation, in a complex with an NS4A co-factor peptide, at 2.5 A resolution. Crystals belong to space group R32 with unit cell dimensions of a=225.31 A, b=225.31 A, c=75.66 A, alpha=90°, beta=90°, and gamma=120° |
| 3.4.21.98 | in complex with inhibitor (4R,6S,7Z,15S,17S)-17-[((8-chloro-7-methoxy-2-[4-(propan-2-yl)-1,3-thiazol-2-yl]quinolin-4-yl)oxy)methyl]-13-methyl-N-[(1-methylcyclopropyl)sulfonyl]-2,14-dioxo-1,3,13-triazatricyclo[13.2.0.0-4,6-]heptadec-7-ene-4-carboxamide, to 2.84 A resolution. Structure shows that the canonical hydrogen bonds between the amide moieties of the inhibitor and the NS3 protease main chain from which amino acids R155 and A157 are involved in hydrogen bond donor/acceptor interactions are maintained |
| 3.4.21.98 | in complex with inhibitor 3-cyclohexyl-2,5-dioxo-12-oxa-1,4-diazatricyclo(11.5.3.016,20)-henicosa-13(21),14,16(20)-triene-18-carboxylic acid ((((1-(dimethylcarbamoylphenylmethyl)carbamoyl)methyl)aminooxalyl)butyl)-amide |
| 3.4.21.98 | in complex with inhibitor N-(tert-butylcarbamoyl)-3-methyl-L-valyl-(4R)-N-[(1R,2S)-1-carboxy-2-ethenylcyclopropyl]-4-[(7-methoxy-2-phenylquinolin-4-yl)oxy]-L-prolinamide. The compound is bound to the active site of HCV protease through an anti-parallel beta-sheet between the inhibitor backbone and the E2-strand of the protease |
| 3.4.21.98 | in complex with inhibitor tert-butyl (1-cyclohexyl-2-[(3R)-3-[(1-[[(2-[[(1S)-2-(dimethylamino)-2-oxo-1-phenylethyl]amino]-2-oxoethyl)amino](oxo)acetyl]pentyl)carbamoyl]-2-azabicyclo[2.2.1]hept-2-yl]-2-oxoethyl)carbamate |
