Research workbench
Crystal structure of HCV NS3-4A V36M mutant
Analyse Crystal structure of HCV NS3-4A V36M mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QV1
- Type
- protein
- Length
- 369 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NS3; Peptide
- UniProt
- A1Z094
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NS3 | protein | 151 | 12% helix, 51% strand | A1Z094 |
| B | NS3 | protein | 181 | 15% helix, 42% strand | A1Z094 |
| C | Peptide | protein | 16 | 0% helix, 56% strand | — |
| D | Peptide | protein | 21 | 0% helix, 48% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.56 | 0.85 | 20 | empty |
| 2 | 50 | 0.38 | 0.81 | 15 | empty |
| 3 | 83 | 0.35 | 0.75 | 19 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1272 Ų buried · 27 hydrogen bonds · protein-protein
- A–C · 880 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 453 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 287 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 203 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2QV1 · Crystal structure of HCV NS3-4A V36M mutant · 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 A1Z094
- Elsewhere: RCSB PDB 2QV1 · PDBe 2QV1 · UniProt A1Z094
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.