Research workbench
Crystal structure of variola virus virulence factor F1L in complex with human bid BH3 domain
Analyse Crystal structure of variola virus virulence factor F1L in complex with human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AJJ
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homolog of vaccinia virus cds F1L putative; BH3-interacting domain death agonist
- UniProt
- Q85365, P55957
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homolog of vaccinia virus cds F1L putative | protein | 138 | 83% helix, 0% strand | Q85365 |
| B | BH3-interacting domain death agonist | protein | 29 | 66% helix, 0% strand | P55957 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.46 | 0.73 | 26 | empty |
| 2 | 117 | 0.43 | 0.76 | 16 | empty |
| 3 | 85 | 0.32 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1123 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5AJJ · Crystal structure of variola virus virulence factor F1L in complex with human Bid BH3… · the same entry in another collection · chain A against A, TM-score 1.00
- P55957 · AlphaFold monomer V2.0 prediction for BH3-interacting domain death agonist (P55957) · a predicted model of the same protein · chain B against A, TM-score 0.64
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 Q85365
- Every structure of UniProt P55957
- Elsewhere: RCSB PDB 5AJJ · PDBe 5AJJ · UniProt Q85365 · UniProt P55957
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