Research workbench
NMR structure of hepatitis C virus NS3 serine protease complexed with the non-covalently bound phenethylamide inhibitor
Analyse NMR structure of hepatitis C virus NS3 serine protease complexed with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K1Q
- Type
- protein
- Length
- 168 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NS3 protease; Phenethylamide
- UniProt
- P90191
- Ligands
- IBU, FE3, ZN
- Pockets
- 3 · best druggability 0.46
Structure
solution nmr · 2 distinct chains · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NS3 protease | protein | 165 | 8% helix, 46% strand | P90191 |
| B | Phenethylamide | protein | 3 | 0% helix, 33% strand | — |
Ligands and binding sites
- IBU · 2-methylpropyl hydrogen carbonate · ligand · chains A, B
- FE3 · 4-(2-aminoethyl)-3-chlorobenzoic acid · ligand · chains A, B
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.46 | 0.83 | 21 | empty |
| 2 | 55 | 0.33 | 0.77 | 15 | empty |
| 3 | 54 | 0.31 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 333 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 1 modified (covalent ligand, nonstandard).
Compared structures
- 2K1Q · NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently… · 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 P90191
- Elsewhere: RCSB PDB 2K1Q · PDBe 2K1Q · UniProt P90191
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