Research workbench
GII.10 vietnam 026 norovirus protruding domain in complex with nanobody nano-26 and nano-85
Analyse GII.10 vietnam 026 norovirus protruding domain in complex with nanobody nano-26… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O04
- Type
- protein
- Length
- 1,076 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5F4T5
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 308 | — | Q5F4T5 |
| B | — | protein | 315 | — | Q5F4T5 |
| E | — | protein | 112 | — | — |
| D | — | protein | 119 | — | — |
| F | — | protein | 101 | — | — |
| C | — | protein | 121 | — | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 18 copies · chains A, B, E, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5O04 · GII.10 Vietnam 026 norovirus protruding domain in complex with Nanobody Nano-26 and… · 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 5O04 · PDBe 5O04 · UniProt Q5F4T5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.