Research workbench
Structural basis for antibody cross-neutralization of respiratory syncytial virus and human metapneumovirus
Analyse Structural basis for antibody cross-neutralization of respiratory syncytial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U68
- Type
- protein
- Length
- 2,043 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera protein of fusion glycoprotein F0 and envelope glycoprotein; MPE8
- UniProt
- P03420, M1E1E4
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Chimera protein of fusion glycoprotein F0 and envelope glycoprotein | protein | 448 | 27% helix, 32% strand | P03420, M1E1E4 |
| E, F, G | MPE8 | protein | 233 | 5% helix, 51% strand | — |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1176 | 0.85 | 0.86 | 137 | empty |
| 2 | 986 | 0.85 | 0.86 | 115 | empty |
| 3 | 842 | 0.84 | 0.87 | 75 | empty |
| 4 | 669 | 0.83 | 0.88 | 84 | empty |
| 5 | 856 | 0.77 | 0.80 | 74 | empty |
Interfaces
9 interfaces between chains.
- A–C · 2236 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 2185 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 2167 Ų buried · 16 hydrogen bonds · protein-protein
- C–G · 1216 Ų buried · 20 hydrogen bonds · protein-protein
- A–E · 1196 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 disulfide (disulfide).
Compared structures
- 5U68 · Structural basis for antibody cross-neutralization of respiratory syncytial virus and… · 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 P03420
- Every structure of UniProt M1E1E4
- Elsewhere: RCSB PDB 5U68 · PDBe 5U68 · UniProt P03420 · UniProt M1E1E4
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