Research workbench
Crystal structure of NS3/4A protease variant A156T in complex with Telaprevir
Analyse Crystal structure of NS3/4A protease variant A156T in complex with Telaprevir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SV9
- Type
- protein
- Length
- 199 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Hepatitis C virus
- Molecule
- NS3 protease, NS4A protein
- UniProt
- A8DG50
- Ligands
- SV6, ZN, SO4
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 13% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NS3 protease, NS4A protein | protein | 199 | 13% helix, 44% strand | A8DG50 |
Ligands and binding sites
- SV6 · (1S,3aR,6aS)-2-[(2S)-2-({(2S)-2-cyclohexyl-2-[(pyrazin-2-ylcarbonyl)amino]acetyl}amino)-3,3-dimethylbutanoyl]-N-[(2R,3S)-1-(cyclopropylamino)-2-hydroxy-1-oxohexan-3-yl]octahydrocyclopenta[c]pyrrole-1-carboxamide · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3SV9 · Crystal structure of NS3/4A protease variant A156T in complex with telaprevir · 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 A8DG50
- Elsewhere: RCSB PDB 3SV9 · PDBe 3SV9 · UniProt A8DG50
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