MolNFT v1 · #185768 · protein
SARS-cov-2 S protein S:A222V + S:D614G mutant 1-up
7QDG: “SARS-cov-2 S protein S:A222V + S:D614G mutant 1-up”. Electron microscopy, 2 ligands (NAG, NDG). MolNFT v1 #185768 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7QDG
- Type
- protein
- Length
- 3,193 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2, P10104
- Ligands
- NAG, NDG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1070 | — | P0DTC2, P10104 |
| B | — | protein | 1049 | — | P0DTC2, P10104 |
| C | — | protein | 1074 | — | P0DTC2, P10104 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 46 copies · chains A, B, C
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7QDG · SARS-CoV-2 S protein S:A222V + S:D614G mutant 1-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
- Every structure of UniProt P10104
- Elsewhere: RCSB PDB 7QDG · PDBe 7QDG · UniProt P0DTC2 · UniProt P10104
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