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Structure of the SARS-cov-2 S 6P trimer in complex with the human neutralizing antibody Fab fragment, BG10-19
Analyse Structure of the SARS-cov-2 S 6P trimer in complex with the human neutralizing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M6E
- Type
- protein
- Length
- 3,795 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG, FUC
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | — | protein | 1034 | — | P0DTC2 |
| D, F, H | — | protein | 123 | — | — |
| C, G, L | — | protein | 108 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 34 copies · chains B, F, A, E, H, D
- FUC · alpha-L-fucopyranose · sugar · chains B, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M6E · Structure of the SARS-CoV-2 S 6P trimer in complex with the human neutralizing antibody… · 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 7M6E · PDBe 7M6E · UniProt P0DTC2
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