Research workbench
Structure of Legionella pneumophila Lcl C-terminal domain bound to sulphate
Analyse Structure of Legionella pneumophila Lcl C-terminal domain bound to sulphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8QK8
- Type
- protein
- Length
- 262 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Legionella pneumophila 130b
- Molecule
- HbP1
- UniProt
- E7BLH6
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HbP1 | protein | 131 | 22% helix, 33% strand | E7BLH6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
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 | 62 | 0.54 | 0.88 | 16 | empty |
| 2 | 53 | 0.29 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 375 Ų buried · 4 hydrogen bonds · protein-protein
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 E7BLH6
- Elsewhere: RCSB PDB 8QK8 · PDBe 8QK8 · UniProt E7BLH6
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