Research workbench
Deerpox virus DPV022 in complex with bak BH3
Analyse Deerpox virus DPV022 in complex with bak BH3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UF1
- Type
- protein
- Length
- 157 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antiapoptotic membrane protein; BCL-2 homologous ANTAGONIST/KILLER
- UniProt
- Q08FF8, Q16611
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antiapoptotic membrane protein | protein | 135 | 79% helix, 0% strand | Q08FF8 |
| B | BCL-2 homologous ANTAGONIST/KILLER | protein | 22 | 73% helix, 0% strand | Q16611 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.52 | 0.74 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 920 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 Q08FF8
- Every structure of UniProt Q16611
- Elsewhere: RCSB PDB 4UF1 · PDBe 4UF1 · UniProt Q08FF8 · UniProt Q16611
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.