Research workbench
Prefusion-stabilized hmpv fusion protein bound to adi-61026 and MPE8 fabs
Analyse Prefusion-stabilized hmpv fusion protein bound to adi-61026 and MPE8 fabs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8CW9
- Type
- protein
- Length
- 2,658 residues
- Chains
- 15
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fusion glycoprotein F0; MPE8 light chain; Adi-61026 heavy; Adi-61026 light; MPE8 heavy…
- UniProt
- H6X1Z0
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 5 distinct chains · 17% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, F | Fusion glycoprotein F0 | protein | 430 | 32% helix, 34% strand | H6X1Z0 |
| B, M, O | MPE8 light chain | protein | 107 | 3% helix, 44% strand | — |
| C, H, I | Adi-61026 heavy | protein | 121 | 2% helix, 47% strand | — |
| D, K, L | Adi-61026 light | protein | 106 | 3% helix, 48% strand | — |
| G, J, N | MPE8 heavy chain | protein | 122 | 5% helix, 51% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, C, E, I, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1010 | 0.84 | 0.85 | 135 | empty |
| 2 | 246 | 0.81 | 0.93 | 42 | empty |
| 3 | 237 | 0.80 | 0.93 | 43 | empty |
| 4 | 1026 | 0.80 | 0.81 | 104 | empty |
| 5 | 612 | 0.79 | 0.84 | 77 | empty |
Interfaces
27 interfaces between chains.
- E–F · 1867 Ų buried · 17 hydrogen bonds · protein-protein
- A–E · 1866 Ų buried · 16 hydrogen bonds · protein-protein
- A–F · 1843 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 886 Ų buried · 14 hydrogen bonds · protein-protein
- I–K · 880 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 45 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 8CW9 · Prefusion-stabilized hMPV fusion protein bound to ADI-61026 and MPE8 Fabs · 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 H6X1Z0
- Elsewhere: RCSB PDB 8CW9 · PDBe 8CW9 · UniProt H6X1Z0
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