Research workbench
Prefusion rsv F bound to RV521
Analyse Prefusion rsv F bound to RV521 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KQD
- Type
- protein
- Length
- 441 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F0
- UniProt
- C3UPB8
- Ligands
- WVA, SO4
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Fusion glycoprotein F0 | protein | 441 | 30% helix, 34% strand | C3UPB8 |
Ligands and binding sites
- WVA · 1'-{[5-(aminomethyl)-1-(4,4,4-trifluorobutyl)-1H-benzimidazol-2-yl]methyl}-6'-fluorospiro[cyclopropane-1,3'-indol]-2'(1'H)-one · ligand · chains F
- SO4 · Sulfate ion · ion · 6 copies · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.59 | 0.83 | 19 | empty |
| 2 | 107 | 0.37 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 7KQD · Prefusion RSV F Bound to RV521 · the same entry in another collection · chain F against F, 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 C3UPB8
- Elsewhere: RCSB PDB 7KQD · PDBe 7KQD · UniProt C3UPB8
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