Research workbench
Structure of the SARS-cov-2 S 6P trimer in complex with the neutralizing antibody Fab fragment, C1717
Analyse Structure of the SARS-cov-2 S 6P trimer in complex with the neutralizing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UAR
- Type
- protein
- Length
- 3,614 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, BMA, FUC
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 968 | — | P0DTC2 |
| B | — | protein | 983 | — | P0DTC2 |
| C | — | protein | 976 | — | P0DTC2 |
| H, D, F | — | protein | 119 | — | — |
| L, E, G | — | protein | 110 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 41 copies · chains A, B, L, C, D, E
- BMA · beta-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7UAR · Structure of the SARS-CoV-2 S 6P trimer in complex with the neutralizing antibody Fab… · 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 7UAR · PDBe 7UAR · UniProt P0DTC2
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