Research workbench
Beta-50 Fab in complex with SARS-cov-2 beta-spike glycoprotein
Analyse Beta-50 Fab in complex with SARS-cov-2 beta-spike glycoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q9F
- Type
- protein
- Length
- 4,312 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, FUC, BMA
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1009 | — | P0DTC2 |
| B | — | protein | 1005 | — | P0DTC2 |
| C | — | protein | 1014 | — | P0DTC2 |
| L, F, K | — | protein | 216 | — | — |
| H, E, J | — | protein | 212 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 59 copies · chains A, L, H, C, B, F, E, K, J
- FUC · alpha-L-fucopyranose · sugar · 3 copies · chains A, H, B, E, C, J
- BMA · beta-D-mannopyranose · sugar · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7Q9F · Beta-50 fab in complex with SARS-CoV-2 beta-Spike glycoprotein · the same entry in another collection · chain C against C, 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 7Q9F · PDBe 7Q9F · UniProt P0DTC2
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