MolNFT v1 · #181566 · protein
South african (B.1.351) SARS-cov-2 spike protein variant (S-gsas- B.1.351) in the 1-rbd-up conformation
7LYO: “South african (B.1.351) SARS-cov-2 spike protein variant (S-gsas- B.1.351) in the 1-rbd-up conformation”. Electron microscopy, 1 ligand (NAG). MolNFT v1 #181566 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LYO
- Type
- protein
- Length
- 2,982 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 995 | — | P0DTC2 |
| B | — | protein | 995 | — | P0DTC2 |
| C | — | protein | 992 | — | P0DTC2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 40 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LYO · South African (B.1.351) SARS-CoV-2 spike protein variant (S-GSAS-B.1.351) in the 1-RBD-up… · 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 7LYO · PDBe 7LYO · UniProt P0DTC2
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