Research workbench
Cryo-EM MAP of pedv S protein with one protomer in the D0-up conformation while the other two in the D0-up conformation.
Analyse Cryo-EM MAP of pedv S protein with one protomer in the D0-up conformation while… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W73
- Type
- protein
- Length
- 3,672 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1Y0DD46
- Ligands
- NAG, MAN, BMA, FUC
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 1224 | — | A0A1Y0DD46 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 106 copies · chains A, B, C
- MAN · alpha-D-mannopyranose · sugar · 59 copies · chains B, A, C
- BMA · beta-D-mannopyranose · sugar · 43 copies · chains A, B, C
- FUC · alpha-L-fucopyranose · sugar · 9 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7W73 · Cryo-EM map of PEDV S protein with one protomer in the D0-up conformation while the other… · 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 A0A1Y0DD46
- Elsewhere: RCSB PDB 7W73 · PDBe 7W73 · UniProt A0A1Y0DD46
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