Research workbench
Crystal structure of the C-terminal domain of ebola virus VP30
Analyse Crystal structure of the C-terminal domain of ebola virus VP30 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I8B
- Type
- protein
- Length
- 259 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Minor nucleoprotein VP30
- UniProt
- Q05323
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Minor nucleoprotein VP30 | protein | 127 | 70% helix, 4% strand | Q05323 |
| B | Minor nucleoprotein VP30 | protein | 132 | 70% helix, 4% strand | Q05323 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.75 | 0.92 | 26 | empty |
| 2 | 80 | 0.44 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1945 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2I8B · Crystal structure of the C-terminal domain of Ebola virus VP30 · 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 Q05323
- Elsewhere: RCSB PDB 2I8B · PDBe 2I8B · UniProt Q05323
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