Research workbench
The secret domain from ectromelia virus
Analyse The secret domain from ectromelia virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ON9
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tumour necrosis factor receptor
- UniProt
- Q7TDW8
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Tumour necrosis factor receptor | protein | 160 | 2% helix, 47% strand | Q7TDW8 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.74 | 0.88 | 28 | empty |
| 2 | 399 | 0.65 | 0.79 | 60 | empty |
Interfaces
1 interface between chains.
- A–B · 1246 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 3ON9 · The SECRET domain from Ectromelia virus · 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 Q7TDW8
- Elsewhere: RCSB PDB 3ON9 · PDBe 3ON9 · UniProt Q7TDW8
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