Research workbench
Cchfv gc prefusion monomer bound to adi-36121 and adi-37801 fabs
Analyse Cchfv gc prefusion monomer bound to adi-36121 and adi-37801 fabs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L7R
- Type
- protein
- Length
- 1,207 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adi-36121 Fab light chain; Adi-36121 Fab heavy chain; Adi-37801 Fab light chain…
- UniProt
- Q8JSZ3
- Ligands
- NAG, BMA
- Pockets
- 17 · best druggability 0.75
Structure
x-ray diffraction · 5 distinct chains · 7% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adi-36121 Fab light chain | protein | 213 | 6% helix, 51% strand | — |
| B | Adi-36121 Fab heavy chain | protein | 215 | 10% helix, 51% strand | — |
| C | Adi-37801 Fab light chain | protein | 205 | 6% helix, 48% strand | — |
| D | Adi-37801 Fab heavy chain | protein | 209 | 7% helix, 54% strand | — |
| G | Glycoprotein C | protein | 365 | 5% helix, 50% strand | Q8JSZ3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains G
- BMA · beta-D-mannopyranose · sugar · chains G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.75 | 0.98 | 27 | empty |
| 2 | 242 | 0.67 | 0.84 | 32 | empty |
| 3 | 239 | 0.48 | 0.74 | 32 | empty |
| 4 | 250 | 0.48 | 0.74 | 33 | empty |
| 5 | 50 | 0.48 | 0.87 | 21 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1865 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1849 Ų buried · 16 hydrogen bonds · protein-protein
- B–G · 668 Ų buried · 4 hydrogen bonds · protein-protein
- D–G · 438 Ų buried · 5 hydrogen bonds · protein-protein
- A–G · 418 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 7L7R · CCHFV Gc prefusion monomer bound to ADI-36121 and ADI-37801 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 Q8JSZ3
- Elsewhere: RCSB PDB 7L7R · PDBe 7L7R · UniProt Q8JSZ3
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