Research workbench
Crystal structure of HCV NS3/4A protease in complex with voxilaprevir
Analyse Crystal structure of HCV NS3/4A protease in complex with voxilaprevir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NZT
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HCV NS3/4A protease
- UniProt
- S4UY05
- Ligands
- L9P, ZN, SO4
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HCV NS3/4A protease | protein | 191 | 14% helix, 46% strand | S4UY05 |
Ligands and binding sites
- L9P · Voxilaprevir · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.39 | 0.81 | 15 | empty |
| 2 | 53 | 0.29 | 0.75 | 15 | empty |
Compared structures
- 6NZT · Crystal structure of HCV NS3/4A protease in complex with voxilaprevir · 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 S4UY05
- Elsewhere: RCSB PDB 6NZT · PDBe 6NZT · UniProt S4UY05
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