Research workbench
SARS spike glycoprotein, stabilized variant, C3 symmetry
Analyse SARS spike glycoprotein, stabilized variant, C3 symmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CRV
- Type
- protein
- Length
- 2,643 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike GLYCOPROTEIN,FIBRITIN
- UniProt
- P59594, D9IEJ2
- Ligands
- NAG, BMA
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · 1 distinct chain · 22% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Spike GLYCOPROTEIN,FIBRITIN | protein | 881 | 22% helix, 39% strand | P59594, D9IEJ2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 36 copies · chains A, C, B
- BMA · beta-D-mannopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1113 | 0.89 | 0.91 | 131 | empty |
| 2 | 1153 | 0.86 | 0.87 | 130 | empty |
| 3 | 878 | 0.77 | 0.80 | 98 | empty |
| 4 | 526 | 0.74 | 0.82 | 61 | empty |
| 5 | 367 | 0.71 | 0.83 | 29 | empty |
Interfaces
3 interfaces between chains.
- A–C · 4504 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 4470 Ų buried · 40 hydrogen bonds · protein-protein
- B–C · 4467 Ų buried · 44 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 33 disulfide, 27 glycan (disulfide, N-glycosylation).
Compared structures
- 6CRV · SARS Spike Glycoprotein, Stabilized variant, C3 symmetry · the same entry in another collection · chain C against C, TM-score 1.00
- 3SCK · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain A against E, TM-score 0.11
- 3SCK · Crystal structure of spike protein receptor-binding domain from a predicted SARS… · a predicted model of the same protein · chain A against E, TM-score 0.11
- 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 0.11
- 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 0.11
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
- Every structure of UniProt D9IEJ2
- Elsewhere: RCSB PDB 6CRV · PDBe 6CRV · UniProt P59594 · UniProt D9IEJ2
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