Research workbench
Domain swapped bromodomain from leishmania donovani
Analyse Domain swapped bromodomain from leishmania donovani in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FEA
- Type
- protein
- Length
- 246 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- E9BU61
- Ligands
- BMF, BR
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 125 | 68% helix, 0% strand | E9BU61 |
| B | Uncharacterized protein | protein | 121 | 74% helix, 0% strand | E9BU61 |
Ligands and binding sites
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 | 683 | 0.78 | 0.82 | 50 | BMF, BR |
Interfaces
1 interface between chains.
- A–B · 2907 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 5FEA · Domain Swapped Bromodomain from Leishmania donovani · 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 E9BU61
- Elsewhere: RCSB PDB 5FEA · PDBe 5FEA · UniProt E9BU61
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.