Research workbench
Structure of HCV NS5B bound to an anthranilic acid inhibitor
Analyse Structure of HCV NS5B bound to an anthranilic acid inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QE2
- Type
- protein
- Length
- 1,044 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase
- EC
- 2.7.7.48
- UniProt
- Q99AU2
- Ligands
- 452
- Pockets
- 15 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase (EC 2.7.7.48) | protein | 521 | 50% helix, 15% strand | Q99AU2 |
| B | RNA-directed RNA polymerase (EC 2.7.7.48) | protein | 523 | 51% helix, 15% strand | Q99AU2 |
Ligands and binding sites
- 452 · 2-{[N-(2-acetyl-5-chloro-4-fluorophenyl)glycyl]amino}benzoic acid · ligand · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1108 | 0.80 | 0.81 | 91 | 452 |
| 2 | 973 | 0.79 | 0.81 | 82 | 452 |
| 3 | 994 | 0.78 | 0.80 | 78 | empty |
| 4 | 98 | 0.48 | 0.80 | 20 | empty |
| 5 | 62 | 0.47 | 0.84 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 646 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2QE2 · Structure of HCV NS5B Bound to an Anthranilic Acid Inhibitor · 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 Q99AU2
- Elsewhere: RCSB PDB 2QE2 · PDBe 2QE2 · UniProt Q99AU2
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