Research workbench
Cryo-EM structure of SARS-cov-2 spike D614G variant, one rbd-up conformation 1
Analyse Cryo-EM structure of SARS-cov-2 spike D614G variant, one rbd-up conformation 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EAZ
- Type
- protein
- Length
- 3,051 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike glycoprotein
- UniProt
- P0DTC2
- Ligands
- NAG, BMA
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 22% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spike glycoprotein | protein | 1013 | 23% helix, 26% strand | P0DTC2 |
| B | Spike glycoprotein | protein | 1020 | 21% helix, 27% strand | P0DTC2 |
| C | Spike glycoprotein | protein | 1018 | 22% helix, 27% strand | P0DTC2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 80 copies · chains A, C, B
- BMA · beta-D-mannopyranose · sugar · 2 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 | 1134 | 0.87 | 0.88 | 133 | empty |
| 2 | 556 | 0.85 | 0.90 | 69 | empty |
| 3 | 1126 | 0.81 | 0.83 | 97 | empty |
| 4 | 1173 | 0.79 | 0.81 | 96 | empty |
| 5 | 813 | 0.75 | 0.79 | 62 | empty |
Interfaces
3 interfaces between chains.
- B–C · 4309 Ų buried · 34 hydrogen bonds · protein-protein
- A–C · 4241 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 4099 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 45 glycan, 36 disulfide (N-glycosylation, disulfide).
Compared structures
- 7EAZ · Cryo-EM structure of SARS-CoV-2 Spike D614G variant, one RBD-up conformation 1 · 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 7EAZ · PDBe 7EAZ · UniProt P0DTC2
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