Research workbench
Crystal structure of the murine norovirus VP1 P domain in complex with the CD300LF receptor and glycochenodeoxycholic acid
Analyse Crystal structure of the murine norovirus VP1 P domain in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E47
- Type
- protein
- Length
- 825 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q80J94, Q6SJQ7
- Ligands
- CHO, MG
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 302 | — | Q80J94 |
| F | — | protein | 109 | — | Q6SJQ7 |
| G | — | protein | 112 | — | Q6SJQ7 |
Ligands and binding sites
- CHO · Glycochenodeoxycholic acid · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 6 copies · chains A, B, F, G
- EDO · 1,2-ethanediol · additive · 22 copies · chains A, B, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q6SJQ7 · AlphaFold monomer V2.0 prediction for CMRF35-like molecule 1 (Q6SJQ7) · a predicted model of the same protein · chain F 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 Q80J94
- Every structure of UniProt Q6SJQ7
- Elsewhere: RCSB PDB 6E47 · PDBe 6E47 · UniProt Q80J94 · UniProt Q6SJQ7
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