MolNFT v1 · #182717 · protein
Structural basis for enhanced infectivity and immune evasion of SARS- cov-2 variants
7N1V: “Structural basis for enhanced infectivity and immune evasion of SARS- cov-2 variants”. Electron microscopy, 3 ligands (NAG, MAN, FUC). MolNFT v1 #182717 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7N1V
- Type
- protein
- Length
- 3,274 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, MAN, FUC
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1089 | — | P0DTC2 |
| B | — | protein | 1091 | — | P0DTC2 |
| C | — | protein | 1094 | — | P0DTC2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 86 copies · chains A, B, C
- MAN · alpha-D-mannopyranose · sugar · 6 copies
- FUC · alpha-L-fucopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N1V · Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants · 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 P0DTC2
- Elsewhere: RCSB PDB 7N1V · PDBe 7N1V · UniProt P0DTC2
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