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Crystal structure of hepatis C virus protease (NS3) complexed with tripeptidic acyl sulfonamide inhibitor (compound 18)
Analyse Crystal structure of hepatis C virus protease (NS3) complexed with tripeptidic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BQK
- Type
- protein
- Length
- 386 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NS3 protease
- UniProt
- A0A075D220
- Ligands
- Z1E, ZN
- Pockets
- 4 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NS3 protease | protein | 193 | 14% helix, 46% strand | A0A075D220 |
Ligands and binding sites
- Z1E · N-(tert-butoxycarbonyl)-3-methyl-L-valyl-(4R)-4-[(7-chloro-4-methoxyisoquinolin-1-yl)oxy]-N-[(1R,2R)-1-[(cyclopropylsulfonyl)carbamoyl]-2-(difluoromethyl) cyclopropyl]-L-prolinamide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.35 | 0.78 | 16 | empty |
| 2 | 78 | 0.35 | 0.76 | 16 | empty |
| 3 | 76 | 0.35 | 0.75 | 16 | empty |
| 4 | 78 | 0.34 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 187 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6BQK · Crystal structure of hepatis C virus protease (NS3) complexed with tripeptidic acyl… · 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 A0A075D220
- Elsewhere: RCSB PDB 6BQK · PDBe 6BQK · UniProt A0A075D220
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