Research workbench
Cryo-EM structure of the SARS-cov-2 HR1HR2 fusion core complex with V1176F mutation
Analyse Cryo-EM structure of the SARS-cov-2 HR1HR2 fusion core complex with V1176F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RZV
- Type
- protein
- Length
- 339 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SARS-cov-2 HR1 linked to a SCAFFOLD,SPIKE protein S2'; Spike protein S2'
- UniProt
- P0DTC2
Structure
electron microscopy · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | SARS-cov-2 HR1 linked to a SCAFFOLD,SPIKE protein S2' | protein | 71 | 97% helix, 0% strand | P0DTC2 |
| D, E, F | Spike protein S2' | protein | 42 | 40% helix, 0% strand | P0DTC2 |
Interfaces
9 interfaces between chains.
- A–D · 1384 Ų buried · 19 hydrogen bonds · protein-protein
- B–E · 1382 Ų buried · 19 hydrogen bonds · protein-protein
- C–F · 1379 Ų buried · 19 hydrogen bonds · protein-protein
- C–E · 1225 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1224 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7RZV · Cryo-EM structure of the SARS-CoV-2 HR1HR2 fusion core complex with V1176F 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 7RZV · PDBe 7RZV · UniProt P0DTC2
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