MolNFT v2 · #151546 · protein
Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid protein
6GY9: “Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid protein”. X-ray diffraction at 1.83, 1 ligand (KBA). MolNFT v2 #151546 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GY9
- Type
- protein
- Length
- 613 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.83
- Source
- Norwalk virus
- UniProt
- Q5F4T5
- Ligands
- KBA
Structure
x-ray diffraction · resolution 1.83 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 314 | — | Q5F4T5 |
| B | — | protein | 299 | — | Q5F4T5 |
Ligands and binding sites
- KBA · 2-(1H-1,2,3-triazol-1-yl)ethyl 6-deoxy-alpha-L-galactopyranoside · sugar · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GY9 · Fucose-functionalized precision glycomacromolecules targeting human norovirus capsid… · 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 Q5F4T5
- Elsewhere: RCSB PDB 6GY9 · PDBe 6GY9 · UniProt Q5F4T5
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