Research workbench
Cryo-EM structure of prefusion SARS-cov-2 spike glycoprotein in complex with 910-30 Fab
Analyse Cryo-EM structure of prefusion SARS-cov-2 spike glycoprotein in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KS9
- Type
- protein
- Length
- 3,189 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | — | protein | 107 | — | — |
| H | — | protein | 112 | — | — |
| A | — | protein | 992 | — | P0DTC2 |
| B | — | protein | 987 | — | P0DTC2 |
| C | — | protein | 991 | — | P0DTC2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 59 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7KS9 · Cryo-EM structure of prefusion SARS-CoV-2 spike glycoprotein in complex with 910-30 Fab · the same entry in another collection · chain L against L, 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 7KS9 · PDBe 7KS9 · UniProt P0DTC2
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