Research workbench
A SARS-cov-2 neutralizing antibody
Analyse A SARS-cov-2 neutralizing antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F0X
- Type
- protein
- Length
- 411 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spike protein S1; Antibody
- UniProt
- P0DTC2
- Pockets
- 4 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spike protein S1 | protein | 183 | 16% helix, 29% strand | P0DTC2 |
| B | Antibody | protein | 228 | 4% helix, 49% strand | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.51 | 0.78 | 24 | empty |
| 2 | 83 | 0.35 | 0.75 | 17 | empty |
| 3 | 66 | 0.34 | 0.77 | 17 | empty |
| 4 | 61 | 0.30 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 598 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7F0X · A SARS-CoV-2 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 7F0X · PDBe 7F0X · UniProt P0DTC2
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