Research workbench
SARS-cov-2 omicron variant S trimer complexed with two JMB2002 Fab
Analyse SARS-cov-2 omicron variant S trimer complexed with two JMB2002 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WPE
- Type
- protein
- Length
- 4,187 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DTC2
- Ligands
- NAG
Structure
electron microscopy · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1021 | — | P0DTC2 |
| B | — | protein | 1024 | — | P0DTC2 |
| C | — | protein | 1024 | — | P0DTC2 |
| X, U | — | protein | 225 | — | — |
| Y, V | — | protein | 214 | — | — |
| Z, W | — | protein | 120 | — | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 40 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WPE · SARS-CoV-2 Omicron Variant S Trimer complexed with two JMB2002 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 7WPE · PDBe 7WPE · UniProt P0DTC2
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