Research workbench
Fic domain of BEP1 from bartonella rochalimae in complex with biaa
Analyse Fic domain of BEP1 from bartonella rochalimae in complex with biaa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EU0
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bartonella effector protein (bep) substrate of virb T4SS; Antitoxin 1
- UniProt
- E6YJU0, E6YLF5
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 57% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bartonella effector protein (bep) substrate of virb T4SS | protein | 213 | 53% helix, 7% strand | E6YJU0 |
| B | Antitoxin 1 | protein | 55 | 71% helix, 0% strand | E6YLF5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.70 | 0.81 | 46 | SO4 |
| 2 | 117 | 0.46 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1139 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5EU0 · FIC domain of Bep1 from Bartonella rochalimae in complex with BiaA · 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 E6YJU0
- Every structure of UniProt E6YLF5
- Elsewhere: RCSB PDB 5EU0 · PDBe 5EU0 · UniProt E6YJU0 · UniProt E6YLF5
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