Research workbench
Cell attachment protein VP8* of a human rotavirus specifically interacts with a-type histo-blood group antigen
Analyse Cell attachment protein VP8* of a human rotavirus specifically interacts with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DRV
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer capsid protein VP4
- UniProt
- Q86169
- Ligands
- GLA, FUC, A2G
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer capsid protein VP4 | protein | 163 | 8% helix, 56% strand | Q86169 |
Ligands and binding sites
- GLA · alpha-D-galactopyranose · sugar · chains A
- FUC · alpha-L-fucopyranose · sugar
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4DRV · Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type… · 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 Q86169
- Elsewhere: RCSB PDB 4DRV · PDBe 4DRV · UniProt Q86169
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