Research workbench
The molecular structure of toll-like receptor 3 ligand binding domain
Analyse The molecular structure of toll-like receptor 3 ligand binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A0Z
- Type
- protein
- Length
- 671 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Toll-like receptor 3
- UniProt
- O15455
- Ligands
- NAG, BMA, FUC, GLC, MAN, NDG, SO4
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toll-like receptor 3 | protein | 671 | 10% helix, 17% strand | O15455 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 20 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 3 copies
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- MAN · alpha-D-mannopyranose · sugar
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar
- SO4 · Sulfate ion · ion · 3 copies · chains A
- BME · Beta-mercaptoethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 11 glycan, 4 disulfide, 1 covalent (N-glycosylation, disulfide, additive adduct).
Compared structures
- 2A0Z · The molecular structure of toll-like receptor 3 ligand binding domain · the same entry in another collection · chain A against A, TM-score 1.00
- O15455 · AlphaFold monomer V2.0 prediction for toll-like receptor 3 (O15455) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O15455
- Elsewhere: RCSB PDB 2A0Z · PDBe 2A0Z · UniProt O15455
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