MolNFT v1 · #181544 · protein
SARS-cov-2 S/S2M11/S2M28 global refinement
7LY2: “SARS-cov-2 S/S2M11/S2M28 global refinement”. Electron microscopy, 3 ligands (NAG, BMA, FUC). MolNFT v1 #181544 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LY2
- Type
- protein
- Length
- 4,470 residues
- Chains
- 15
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, BMA, FUC
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, J | — | protein | 1041 | — | P0DTC2 |
| D, C, K | — | protein | 104 | — | — |
| E, F, M | — | protein | 122 | — | — |
| H, G, N | — | protein | 117 | — | — |
| L, I, O | — | protein | 106 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 63 copies · chains A, C, B, K, D, J, H, G, N
- BMA · beta-D-mannopyranose · sugar · 3 copies
- FUC · alpha-L-fucopyranose · sugar · 3 copies · chains A, F, B, M, E, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 7LY2 · PDBe 7LY2 · UniProt P0DTC2
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