Research workbench
Crystal structure of prefusion-stabilized rsv F variant ds-CAV1 at pH 5.5
Analyse Crystal structure of prefusion-stabilized rsv F variant ds-CAV1 at pH 5.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MMU
- Type
- protein
- Length
- 455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F2; Fusion glycoprotein F1 fused with fibritin trimerization domain
- UniProt
- P03420, P10104
- Ligands
- NAG, SO4, PO4
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fusion glycoprotein F2 | protein | 82 | 28% helix, 33% strand | P03420 |
| B | Fusion glycoprotein F1 fused with fibritin trimerization domain | protein | 373 | 31% helix, 31% strand | P03420, P10104 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains B
- SO4 · Sulfate ion · ion · 4 copies · chains B
- PO4 · Phosphate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.45 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 4424 Ų buried · 82 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 4MMU · Crystal Structure of Prefusion-stabilized RSV F Variant DS-Cav1 at pH 5.5 · 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 P10104
- Elsewhere: RCSB PDB 4MMU · PDBe 4MMU · UniProt P03420 · UniProt P10104
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.