Research workbench
Structure of HCV E2 glycoprotein antigenic epitope II bound to the broadly neutralizing antibody HC84-26
Analyse Structure of HCV E2 glycoprotein antigenic epitope II bound to the broadly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ERW
- Type
- protein
- Length
- 434 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-HCV E2 Fab HC84-26 heavy chain; Anti-HCV E2 Fab HC84-26 light chain; HCV E2…
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-HCV E2 Fab HC84-26 heavy chain | protein | 212 | 3% helix, 53% strand | — |
| B | Anti-HCV E2 Fab HC84-26 light chain | protein | 213 | 9% helix, 48% strand | — |
| C | HCV E2 glycoprotein epitope II | protein | 9 | 0% helix, 0% strand | — |
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 | 612 | 0.64 | 0.75 | 59 | empty |
| 2 | 124 | 0.36 | 0.73 | 17 | empty |
| 3 | 52 | 0.26 | 0.73 | 11 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1890 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 375 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 296 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 5ERW · Structure of HCV E2 glycoprotein antigenic Epitope II bound to the broadly neutralizing… · 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
- Elsewhere: RCSB PDB 5ERW · PDBe 5ERW
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