Research workbench
Cryo-EM structure of the SARS-cov-2 HR1HR2 fusion core complex with L938F mutation
Analyse Cryo-EM structure of the SARS-cov-2 HR1HR2 fusion core complex with L938F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RZS
- Type
- protein
- Length
- 324 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SARS-cov-2 HR1 L938F linked to a SCAFFOLD,SPIKE protein S2'; Spike protein S2'
- UniProt
- P0DTC2
Structure
electron microscopy · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | SARS-cov-2 HR1 L938F linked to a SCAFFOLD,SPIKE protein S2' | protein | 71 | 97% helix, 0% strand | P0DTC2 |
| D, E, F | Spike protein S2' | protein | 37 | 46% helix, 0% strand | P0DTC2 |
Interfaces
9 interfaces between chains.
- C–F · 1189 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1187 Ų buried · 15 hydrogen bonds · protein-protein
- B–E · 1186 Ų buried · 15 hydrogen bonds · protein-protein
- C–E · 1150 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 1150 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7RZS · Cryo-EM structure of the SARS-CoV-2 HR1HR2 fusion core complex with L938F mutation · 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 7RZS · PDBe 7RZS · UniProt P0DTC2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.