Research workbench
Crystal structure of mouse TLR9 (unliganded form)
Analyse Crystal structure of mouse TLR9 (unliganded form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WPF
- Type
- protein
- Length
- 740 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.959
- Source
- Mus musculus
- Molecule
- Toll-like receptor 9
- UniProt
- Q9EQU3
- Ligands
- NAG, SO4
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · resolution 1.959 · 1 distinct chain · 10% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toll-like receptor 9 | protein | 740 | 10% helix, 17% strand | Q9EQU3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- SO4 · Sulfate ion · ion · 12 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.53 | 0.86 | 19 | SO4 |
| 2 | 135 | 0.39 | 0.74 | 33 | empty |
| 3 | 78 | 0.35 | 0.76 | 19 | empty |
Modifications
Observed in the structure: 8 disulfide, 3 glycan (disulfide, N-glycosylation).
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 Q9EQU3
- Elsewhere: RCSB PDB 3WPF · PDBe 3WPF · UniProt Q9EQU3
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