Research workbench
Cryo-EM structure of the SARS-CoV-2 Omicron HR1-42G complex
Analyse Cryo-EM structure of the SARS-CoV-2 Omicron HR1-42G complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8FA2
- Type
- protein
- Length
- 342 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.82
- Source
- Nostoc punctiforme PCC 73102; Severe acute respiratory syndrome coronavirus 2
- Molecule
- Scaffolded Spike protein S2' HR1; Spike protein S2' 42G
- UniProt
- B2J981, P0DTC2
Structure
electron microscopy · resolution 2.82 · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Scaffolded Spike protein S2' HR1 | protein | 71 | 97% helix, 0% strand | B2J981, P0DTC2 |
| D, E, F | Spike protein S2' 42G | protein | 43 | 44% helix, 0% strand | P0DTC2 |
Interfaces
9 interfaces between chains.
- B–E · 1260 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 1258 Ų buried · 16 hydrogen bonds · protein-protein
- C–F · 1257 Ų buried · 16 hydrogen bonds · protein-protein
- C–E · 1247 Ų buried · 13 hydrogen bonds · protein-protein
- A–F · 1246 Ų buried · 13 hydrogen bonds · protein-protein
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 B2J981
- Every structure of UniProt P0DTC2
- Elsewhere: RCSB PDB 8FA2 · PDBe 8FA2 · UniProt B2J981 · UniProt P0DTC2
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