Research workbench
Cryo-EM structure of S protein trimer of SARS-COV2
Analyse Cryo-EM structure of S protein trimer of SARS-COV2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FG7
- Type
- protein
- Length
- 1,114 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike glycoprotein
- UniProt
- P0DTC2
- Pockets
- 16 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 20% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spike glycoprotein | protein | 1114 | 20% helix, 24% strand | P0DTC2 |
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.72 | 0.95 | 19 | empty |
| 2 | 147 | 0.70 | 0.89 | 31 | empty |
| 3 | 618 | 0.66 | 0.76 | 71 | empty |
| 4 | 176 | 0.65 | 0.85 | 34 | empty |
| 5 | 77 | 0.57 | 0.87 | 19 | empty |
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 7FG7 · Cryo-EM structure of S protein trimer of SARS-CoV2 · 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 7FG7 · PDBe 7FG7 · UniProt P0DTC2
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