Research workbench
Dpbb domain of vcp-like ATPase from thermoplasma acidophilum
Analyse Dpbb domain of vcp-like ATPase from thermoplasma acidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DBO
- Type
- protein
- Length
- 177 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vcp-like ATPase
- UniProt
- O05209
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vcp-like ATPase | protein | 91 | 19% helix, 35% strand | O05209 |
| B | Vcp-like ATPase | protein | 86 | 20% helix, 37% strand | O05209 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.31 | 0.75 | 13 | empty |
| 2 | 55 | 0.24 | 0.72 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 545 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
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 O05209
- Elsewhere: RCSB PDB 7DBO · PDBe 7DBO · UniProt O05209
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.