MolNFT v1 · #177281 · protein
Cryo-EM structure of SARS-cov-2 S-uk variant (B.1.1.7), one rbd-up conformation 2
7EDG: “Cryo-EM structure of SARS-cov-2 S-uk variant (B.1.1.7), one rbd-up conformation 2”. Electron microscopy, 2 ligands (NAG, BMA). MolNFT v1 #177281 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7EDG
- Type
- protein
- Length
- 3,023 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, BMA
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1015 | — | P0DTC2 |
| B | — | protein | 1000 | — | P0DTC2 |
| C | — | protein | 1008 | — | P0DTC2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 78 copies · chains A, B, C
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EDG · Cryo-EM structure of SARS-CoV-2 S-UK variant (B.1.1.7), one RBD-up conformation 2 · 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 7EDG · PDBe 7EDG · UniProt P0DTC2
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