Research workbench
Structural basis of glycan recognition in neonate-specific rotaviruses
Analyse Structural basis of glycan recognition in neonate-specific rotaviruses in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YG0
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer capsid protein VP4
- UniProt
- B6RGK2
- Ligands
- GAL, BGC, NAG
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer capsid protein VP4 | protein | 164 | 8% helix, 52% strand | B6RGK2 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A
- BGC · beta-D-glucopyranose · sugar
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4YG0 · Structural basis of glycan recognition in neonate-specific rotaviruses · 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 B6RGK2
- Elsewhere: RCSB PDB 4YG0 · PDBe 4YG0 · UniProt B6RGK2
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