Research workbench
Cryo-EM structure of human TLR3 in complex with UNC93B1
Analyse Cryo-EM structure of human TLR3 in complex with UNC93B1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C76
- Type
- protein
- Length
- 1,174 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15455, Q9H1C4
- Ligands
- NAG, BMA
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 691 | — | O15455 |
| B | — | protein | 483 | — | Q9H1C4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 23 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7C76 · Cryo-EM structure of human TLR3 in complex with UNC93B1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H1C4 · AlphaFold monomer V2.0 prediction for protein unc-93 homolog B1 (Q9H1C4) · a predicted model of the same protein · chain B against A, TM-score 0.99
- 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 0.97
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
- Every structure of UniProt Q9H1C4
- Elsewhere: RCSB PDB 7C76 · PDBe 7C76 · UniProt O15455 · UniProt Q9H1C4
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