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Structure of the hepatitis C virus strain J4 glycoprotein E2 antigenic region 532-540 bound to the Fab fragment of the non-neutralizing antibody DAO5
Analyse Structure of the hepatitis C virus strain J4 glycoprotein E2 antigenic region… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NPH
- Type
- protein
- Length
- 437 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Genome polyprotein; Heavy chain of Fab fragment derived from non-neutralizing antibody…
- UniProt
- O92972
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Genome polyprotein | protein | 9 | 44% helix, 0% strand | O92972 |
| H | Heavy chain of Fab fragment derived from non-neutralizing antibody DAO5 | protein | 214 | 10% helix, 54% strand | — |
| L | Light chain of Fab fragment derived from non-neutralizing antibody DAO5 | protein | 214 | 6% helix, 51% strand | — |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 516 | 0.63 | 0.75 | 50 | empty |
Interfaces
3 interfaces between chains.
- H–L · 1953 Ų buried · 13 hydrogen bonds · protein-protein
- A–L · 370 Ų buried · 5 hydrogen bonds · protein-protein
- A–H · 324 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5NPH · Structure of the Hepatitis C virus strain J4 glycoprotein E2 antigenic region 532-540… · 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 O92972
- Elsewhere: RCSB PDB 5NPH · PDBe 5NPH · UniProt O92972
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