Research workbench
Crystal structure of hepatitis C virus NS3 helicase inhibitor co- complex with compound 9 [1-(3-ethynylbenzyl)-1H-indol-3-YL]ACETIC acid]
Analyse Crystal structure of hepatitis C virus NS3 helicase inhibitor co- complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OK5
- Type
- protein
- Length
- 861 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease NS3
- UniProt
- K4KA16
- Ligands
- 2T2, CA
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease NS3 | protein | 441 | 31% helix, 21% strand | K4KA16 |
| B | Serine protease NS3 | protein | 420 | 31% helix, 21% strand | K4KA16 |
Ligands and binding sites
- 2T2 · [1-(3-ethynylbenzyl)-1H-indol-3-yl]acetic acid · ligand · chains A
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 908 | 0.84 | 0.86 | 103 | empty |
| 2 | 183 | 0.74 | 0.90 | 35 | empty |
| 3 | 165 | 0.50 | 0.78 | 23 | empty |
| 4 | 150 | 0.44 | 0.75 | 26 | 2T2 |
| 5 | 150 | 0.43 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1199 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4OK5 · Crystal Structure of Hepatitis C Virus NS3 Helicase Inhibitor Co-complex with Compound 9… · 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 K4KA16
- Elsewhere: RCSB PDB 4OK5 · PDBe 4OK5 · UniProt K4KA16
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