MolNFT v1 · #134720 · protein
Crystal structure of prefusion-stabilized bovine rsv F (ds-CAV1 variant: strain ATUE51908)
5TDG · Fusion glycoprotein F0,FIBRITIN: “Crystal structure of prefusion-stabilized bovine rsv F (ds-CAV1 variant: strain ATUE51908)”. X-ray diffraction, 1 ligand (NAG), 14 pockets (best druggability 0.84). MolNFT v1 #134720 on GenesisL1…
- PDB
- 5TDG
- Type
- protein
- Length
- 1,440 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F0,FIBRITIN
- UniProt
- Q9YS24, Q76VI8
- Ligands
- NAG
- Pockets
- 14 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Fusion glycoprotein F0,FIBRITIN | protein | 480 | 31% helix, 34% strand | Q9YS24, Q76VI8 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 905 | 0.84 | 0.86 | 73 | empty |
| 2 | 992 | 0.79 | 0.81 | 86 | empty |
| 3 | 870 | 0.79 | 0.82 | 67 | empty |
| 4 | 1022 | 0.79 | 0.80 | 78 | empty |
| 5 | 484 | 0.78 | 0.85 | 70 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2972 Ų buried · 33 hydrogen bonds · protein-protein
- A–C · 2896 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 2699 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 5TDG · Crystal structure of prefusion-stabilized bovine RSV F (DS-Cav1 variant: strain ATue51908) · 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 Q9YS24
- Every structure of UniProt Q76VI8
- Elsewhere: RCSB PDB 5TDG · PDBe 5TDG · UniProt Q9YS24 · UniProt Q76VI8
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