Research workbench
Structure of the rsv F protein in the post-fusion conformation
Analyse Structure of the rsv F protein in the post-fusion conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RRT
- Type
- protein
- Length
- 1,296 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q84850
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | — | protein | 72 | — | Q84850 |
| B | — | protein | 356 | — | Q84850 |
| D | — | protein | 360 | — | Q84850 |
| F | — | protein | 364 | — | Q84850 |
Compared structures
- 3RRT · Structure of the RSV F protein in the post-fusion conformation · 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 Q84850
- Elsewhere: RCSB PDB 3RRT · PDBe 3RRT · UniProt Q84850
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