Research workbench
Cryo-EM of aedes aegypti TOLL5A dimer bound to SPZ1C
Analyse Cryo-EM of aedes aegypti TOLL5A dimer bound to SPZ1C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B1B
- Type
- protein
- Length
- 1,697 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A6I8TEX2, Q16J57
- Ligands
- NAG, BMA
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 754 | — | A0A6I8TEX2 |
| D | — | protein | 99 | — | Q16J57 |
| P | — | protein | 92 | — | Q16J57 |
| B | — | protein | 752 | — | A0A6I8TEX2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 17 copies · chains A, B, D
- BMA · beta-D-mannopyranose · sugar · 5 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7B1B · Cryo-EM of Aedes Aegypti Toll5A dimer bound to Spz1C · 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 A0A6I8TEX2
- Every structure of UniProt Q16J57
- Elsewhere: RCSB PDB 7B1B · PDBe 7B1B · UniProt A0A6I8TEX2 · UniProt Q16J57
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.