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A structure-based mechanism of SARS virus membrane fusion
Analyse A structure-based mechanism of SARS virus membrane fusion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZVB
- Type
- protein
- Length
- 101 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E2 glycoprotein
- UniProt
- P59594
Structure
x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | E2 glycoprotein | protein | 34 | 88% helix, 0% strand | P59594 |
| B | E2 glycoprotein | protein | 33 | 94% helix, 0% strand | P59594 |
Interfaces
3 interfaces between chains.
- B–C · 611 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 602 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 580 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1ZVB · A structure-based mechanism of SARS virus membrane fusion · the same entry in another collection · chain A against A, TM-score 1.00
- 3SCI · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain B against E, TM-score 0.27
- 3SCI · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain B against E, TM-score 0.27
- 3SCJ · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain B against E, TM-score 0.27
- 3SCJ · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain B against E, TM-score 0.27
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 P59594
- Elsewhere: RCSB PDB 1ZVB · PDBe 1ZVB · UniProt P59594
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