Research workbench
VP8* of P[6] human rotavirus RV3 in complex with LNFP1
Analyse VP8* of P[6] human rotavirus RV3 in complex with LNFP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VX9
- Type
- protein
- Length
- 161 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Outer capsid protein VP4
- UniProt
- D7F7M7
- Ligands
- GAL, BGC, NAG, FUC, SO4
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Outer capsid protein VP4 | protein | 161 | 10% helix, 57% strand | D7F7M7 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VX9 · VP8* of P[6] Human Rotavirus RV3 in complex with LNFP1 · 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 D7F7M7
- Elsewhere: RCSB PDB 5VX9 · PDBe 5VX9 · UniProt D7F7M7
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